|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
9-485 |
0e+00 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 787.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 9 VKNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDEL 88
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 89 AKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLA 168
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 169 IACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKR 248
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 249 VQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPV 328
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 329 IRENHKERTLSYIESGVEEGARLVRDGRED-HAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVA 407
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVkVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1750864354 408 NNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGDLHANGTDGVEFYTRKKMVTARY 485
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-485 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 619.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 5 TVKTVKNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDN 84
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 85 WDELAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWM 164
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 165 FPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGT 243
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 244 ENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDV 323
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 324 FLGPVIRENHKERTLSYIESGVEEGARLVRDGRedHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEA 403
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGR--RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 404 IDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGDLHanGTDGVEFYTRKKMVTA 483
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREG--GREGLEEYTETKTVTI 477
|
..
gi 1750864354 484 RY 485
Cdd:COG1012 478 RL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
17-481 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 567.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 17 WVDSStSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLEN 96
Cdd:pfam00171 1 WVDSE-SETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 97 GKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPdIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFV 176
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLP-SDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 177 LKPSERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGA 255
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 256 KNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKE 335
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 336 RTLSYIESGVEEGARLVRDGREDhavKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANG 415
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAG---LDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1750864354 416 ACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGDlhANGTDGVEFYTRKKMV 481
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGR--EGGPYGLEEYTEVKTV 459
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
9-485 |
0e+00 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 560.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 9 VKNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDEL 88
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 89 AKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLA 168
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 169 IACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKR 248
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 249 VQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVtVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPV 328
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAA-VLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 329 IRENHKERTLSYIESGVEEGARLVRDGReDHAVK--ENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDV 406
Cdd:TIGR01722 320 ITPQAKDRVASLIAGGAAEGAEVLLDGR-GYKVDgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIAL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1750864354 407 ANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGDLHANGTDGVEFYTRKKMVTARY 485
Cdd:TIGR01722 399 INASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
49-483 |
2.19e-167 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 479.01 E-value: 2.19e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 49 DQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQ 128
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 129 LPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVN 208
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 209 G-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCM 287
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 288 AASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGREDHAvkENGYF 367
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEG--GKGYF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 368 VGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAP 447
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 1750864354 448 MAFFPFSGWKDSFYGdlHANGTDGVEFYTRKKMVTA 483
Cdd:cd07078 399 EPSAPFGGVKQSGIG--REGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
11-485 |
3.37e-158 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 457.58 E-value: 3.37e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 11 NYIGGEWVDSSTSLTEPVYNPATG-EVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELA 89
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAI 169
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 170 ACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKR 248
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 249 VQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPV 328
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 329 IRENHKERTLSYIESGVEEGARLVRDG-REDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVA 407
Cdd:cd07131 321 INEAQLEKVLNYNEIGKEEGATLLLGGeRLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1750864354 408 NNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGDLHAnGTDGVEFYTRKKMVTARY 485
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNGHREA-GTTALDAFTEWKAVYVDY 477
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
10-481 |
1.54e-157 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 455.56 E-value: 1.54e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 10 KNYIGGEWVDSSTslTEPVYNPA-TGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDEL 88
Cdd:cd07097 2 RNYIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 89 AKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLA 168
Cdd:cd07097 80 ARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 169 IACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLK 247
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 248 RVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGP 327
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 328 VIRENHKERTLSYIESGVEEGARLVRDGredHAVK--ENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAID 405
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGG---ERLKrpDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 406 VANNSRFANGACIYTDSGASVREFRENIESGMLGVNvgvpAPMA----FFPFSGWKDSFYGdLHANGTDGVEFYTRKKMV 481
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN----LPTAgvdyHVPFGGRKGSSYG-PREQGEAALEFYTTIKTV 471
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
9-485 |
2.51e-155 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 454.59 E-value: 2.51e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 9 VKNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDEL 88
Cdd:PLN02419 114 VPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 89 AKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLA 168
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 169 IACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKR 248
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 249 VQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDvADELISRLVQESNNIVIGNGLEKDVFLGPV 328
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGSEPDADLGPV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 329 IRENHKERTLSYIESGVEEGARLVRDGReDHAVK--ENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDV 406
Cdd:PLN02419 433 ISKQAKERICRLIQSGVDDGAKLLLDGR-DIVVPgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1750864354 407 ANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGDLHANGTDGVEFYTRKKMVTARY 485
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQ 590
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-482 |
2.77e-139 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 407.97 E-value: 2.77e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEV 107
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 108 QRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPM-MV-----PcwmfplAIACGNTFVLKPSE 181
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAaMItrkiaP------ALAAGCTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 182 RTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNG-LLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQ-ALAGaknHS 259
Cdd:cd07103 155 ETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEaLCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSlELGG---NA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 260 --IVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERT 337
Cdd:cd07103 232 pfIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 338 LSYIESGVEEGARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGAC 417
Cdd:cd07103 312 EALVEDAVAKGAKVLTGGK---RLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1750864354 418 IYTDSGASVREFRENIESGMLGVNVGVPA-PMAffPFSGWKDSFYGdlHANGTDGVEFYTRKKMVT 482
Cdd:cd07103 389 VFTRDLARAWRVAEALEAGMVGINTGLISdAEA--PFGGVKESGLG--REGGKEGLEEYLETKYVS 450
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
11-485 |
6.06e-139 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 408.11 E-value: 6.06e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 11 NYIGGEWVDSSTSlTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAK 90
Cdd:cd07086 1 GVIGGEWVGSGGE-TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 91 LVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIA 170
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 171 CGNTFVLKPSERTPLLAARLVELFEEA----GLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENL 246
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 247 KRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLG 326
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 327 PVIRENHKERTLSYIESGVEEGARLVRDG-REDHAvkENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAID 405
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGkRIDGG--EPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 406 VANNSRFANGACIYTDSGASVREFRENIES--GMLGVNVGVPAPMAFFPFSGWKDSfyGDLHANGTDGVEFYTRKKMVTA 483
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNIPTSGAEIGGAFGGEKET--GGGRESGSDAWKQYMRRSTCTI 475
|
..
gi 1750864354 484 RY 485
Cdd:cd07086 476 NY 477
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
28-482 |
6.26e-131 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 386.92 E-value: 6.26e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEAR-GE 106
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 107 VQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRyPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLL 186
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQ-PVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 187 AARLVELFEEAGLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDA 265
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 266 DLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGV 345
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 346 EEGARLVRDGREDH-AVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGA 424
Cdd:cd07093 320 AEGATILTGGGRPElPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1750864354 425 SVREFRENIESGMLGVNvgvpapmAFF------PFSGWKDSfyGDLHANGTDGVEFYTRKKMVT 482
Cdd:cd07093 400 RAHRVARRLEAGTVWVN-------CWLvrdlrtPFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-482 |
2.38e-129 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 383.87 E-value: 2.38e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVP--KRARILFKYQQLLVDNWDELA 89
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDprERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNE-ARGEVQRGIECVEFAAGAPTLMMGKQlpdIATGIESGMY--RYPIGVIGGITPFNFPMMVPCWMFP 166
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKT---IPIDGNFLAYtrREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 167 LAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLL-EHKLVKAISFVGSQPVAEYVYKKGTE- 244
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAIsSHMDVDKIAFTGSTAVGRTIMEAAAKs 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 245 NLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVF 324
Cdd:cd07091 244 NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 325 LGPVIRENHKERTLSYIESGVEEGARLVRDGREdhaVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAI 404
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGER---HGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1750864354 405 DVANNSRFANGACIYTDSGASVREFRENIESGMLGVNV-GVPAPMAffPFSGWKDSFYGdlHANGTDGVEFYTRKKMVT 482
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV--PFGGFKQSGFG--RELGEEGLEEYTQVKAVT 475
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-481 |
1.66e-128 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 381.66 E-value: 1.66e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAF--KGWSKTAVPKRARILFKYQQLLVDNWDELA 89
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLpDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAI 169
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVY-DVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 170 ACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKR 248
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 249 VQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPV 328
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 329 IRENHKERTLSYIESGVEEGARLVRDG-REDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVA 407
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGkRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1750864354 408 NNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPA-PMAffPFSGWKDSFYGdlHANGTDGVEFYTRKKMV 481
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYfAEA--PWGGYKQSGIG--RELGPTGLEEYQETKHI 470
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
28-481 |
1.71e-126 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 375.74 E-value: 1.71e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG--WSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARG 105
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 106 EVQRGIECVEFAAGAPTLMMGKQLPdiatgIESGMY-----RYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPS 180
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIP-----VDKGDYlnftrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 181 ERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHS 259
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGfGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 260 IVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLS 339
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 340 YIESGVEEGARLVRDG-REDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACI 418
Cdd:cd07114 316 YVARAREEGARVLTGGeRPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1750864354 419 YTDSGAsvREFR--ENIESGMLGVNV-GVPAPMAffPFSGWKDSFYGdlHANGTDGVEFYTRKKMV 481
Cdd:cd07114 396 WTRDLA--RAHRvaRAIEAGTVWVNTyRALSPSS--PFGGFKDSGIG--RENGIEAIREYTQTKSV 455
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
12-481 |
2.91e-126 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 375.45 E-value: 2.91e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPM-MVPCWMFPlAIA 170
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFfLIARKLAP-ALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 171 CGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRV 249
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 250 QALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVI 329
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 330 RENHKERTLSYIESGVEEGARLVRDGREDHAvkENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANN 409
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGKRPEG--EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1750864354 410 SRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFpFSGWKDSFYGDlhANGTDGVEFYTRKKMV 481
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGF-HAGWKKSGLGG--ADGKHGLEEYLQTKVV 466
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
53-483 |
1.13e-125 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 370.41 E-value: 1.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 53 QAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDI 132
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 133 ATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHD 212
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 213 VV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASV 291
Cdd:cd06534 161 EVgAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 292 VTVQEDVADELISRLVqesnnivignglekdvflgpvirenhkertlsyiesgveegarlvrdgredhavkengyfvgpT 371
Cdd:cd06534 241 LLVHESIYDEFVEKLV---------------------------------------------------------------T 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 372 IFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFF 451
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEA 337
|
410 420 430
....*....|....*....|....*....|..
gi 1750864354 452 PFSGWKDSFYGDLHanGTDGVEFYTRKKMVTA 483
Cdd:cd06534 338 PFGGVKNSGIGREG--GPYGLEEYTRTKTVVI 367
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
7-485 |
2.13e-123 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 369.63 E-value: 2.13e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 7 KTVKNYIGGEWVDSSTSLtePVYNPA-TGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNW 85
Cdd:cd07124 31 REYPLVIGGKEVRTEEKI--ESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 86 DELAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDiATGIESGmYRY-PIGVIGGITPFNFPMMVPCWM 164
Cdd:cd07124 109 FELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEM-VPGEDNR-YVYrPLGVGAVISPWNFPLAILAGM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 165 FPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKK-- 241
Cdd:cd07124 187 TTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERaa 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 242 ----GTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGN 317
Cdd:cd07124 267 kvqpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 318 GLEKDVFLGPVIRENHKERTLSYIESGVEEGaRLVRDGREDhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRV 397
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVL-ELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 398 KTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPM-AFFPFSGWKDSfyG-DLHANGTDGVEFY 475
Cdd:cd07124 425 KDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALvGRQPFGGFKMS--GtGSKAGGPDYLLQF 502
|
490
....*....|
gi 1750864354 476 TRKKMVTARY 485
Cdd:cd07124 503 MQPKTVTENF 512
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
11-459 |
3.82e-120 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 359.89 E-value: 3.82e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 11 NYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAK 90
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 91 LVTLENGKSFNEARG-EVQRGIECVEFAAGAptlmmgkqLPDIATGIESG---MYRYPIGVIGGITPFNFPM-MVPCWMF 165
Cdd:cd07138 81 AITLEMGAPITLARAaQVGLGIGHLRAAADA--------LKDFEFEERRGnslVVREPIGVCGLITPWNWPLnQIVLKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 166 PlAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTE 244
Cdd:cd07138 153 P-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 245 NLKRV-QALAGaKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDV 323
Cdd:cd07138 232 TVKRVaLELGG-KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 324 FLGPVIRENHKERTLSYIESGVEEGARLVRDGREDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEA 403
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1750864354 404 IDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAffPFSGWKDS 459
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGA--PFGGYKQS 444
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-481 |
8.22e-120 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 358.54 E-value: 8.22e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEV 107
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 108 QRGIECVEFAAGAPTLMMGKQLPdiaTGIESGMY--RYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPL 185
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVP---LPGGSFAYtrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 186 LAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDA 265
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 266 DLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGV 345
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 346 EEGARLVRDGRE--DHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSG 423
Cdd:cd07090 318 QEGAKVLCGGERvvPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1750864354 424 ASVREFRENIESGMLGVNVGVPAPmAFFPFSGWKDSFYGdlHANGTDGVEFYTRKKMV 481
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISP-VEVPFGGYKQSGFG--RENGTAALEHYTQLKTV 452
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
13-481 |
9.69e-119 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 357.46 E-value: 9.69e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 13 IGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLV 92
Cdd:PLN02278 29 IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 93 TLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACG 172
Cdd:PLN02278 109 TLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 173 NTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQA 251
Cdd:PLN02278 189 CTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGdAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 252 LAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRE 331
Cdd:PLN02278 269 ELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 332 NHKERTLSYIESGVEEGARLVRDGredHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSR 411
Cdd:PLN02278 349 AAVQKVESHVQDAVSKGAKVLLGG---KRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTE 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1750864354 412 FANGACIYTDSGASVREFRENIESGMLGVNVG-VPAPMAffPFSGWKDSFYGdlHANGTDGVEFYTRKKMV 481
Cdd:PLN02278 426 AGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGlISTEVA--PFGGVKQSGLG--REGSKYGIDEYLEIKYV 492
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
12-481 |
1.06e-118 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 356.72 E-value: 1.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG-WSKTAVPKRARILFKYQQLLVDNWDELAK 90
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 91 LVTLENGKSFNE-ARGEVQRGIECVEFAAGAPTLMMGKQlpdIATGIESGMY--RYPIGVIGGITPFNFPMMVPCWMFPL 167
Cdd:cd07144 91 IEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKT---IPTSPNKLAYtlHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 168 AIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENL 246
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 247 KRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESN-NIVIGNGLEKDVFL 325
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 326 GPVIRENHKERTLSYIESGVEEGARLVRDGREDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAID 405
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 406 VANNSRFANGACIYTDSGASVREFRENIESGMLGVN------VGVpapmaffPFSGWKDSFYG-DLhanGTDGVEFYTRK 478
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINssndsdVGV-------PFGGFKMSGIGrEL---GEYGLETYTQT 477
|
...
gi 1750864354 479 KMV 481
Cdd:cd07144 478 KAV 480
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
27-482 |
1.14e-117 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 353.05 E-value: 1.14e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 27 PVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGE 106
Cdd:cd07149 2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 107 VQRGIECVEFAAGAPTLMMGKQLP-DIATGIESGM---YRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSER 182
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGETIPfDASPGGEGRIgftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 183 TPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGteNLKRVQALAGAKNHSIV 261
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGsGETVGDALVTDPRVRMISFTGSPAVGEAIARKA--GLKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 262 LNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYI 341
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 342 ESGVEEGARLVRDGREDhavkenGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTD 421
Cdd:cd07149 320 EEAVEGGARLLTGGKRD------GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1750864354 422 SGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSfygdlhANGTDGVEF----YTRKKMVT 482
Cdd:cd07149 394 DLQKALKAARELEVGGVMINDSSTFRVDHMPYGGVKES------GTGREGPRYaieeMTEIKLVC 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
30-481 |
4.18e-117 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 351.74 E-value: 4.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 30 NPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARG-EVQ 108
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 109 RGIECVEFAAGAPTLMMGKQLPdIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAA 188
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 189 RLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADL 267
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 268 NVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGVEE 347
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 348 GARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVR 427
Cdd:cd07115 322 GARLLTGGK---RPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1750864354 428 EFRENIESGMLGVNVgVPAPMAFFPFSGWKDSFYGdlHANGTDGVEFYTRKKMV 481
Cdd:cd07115 399 RVAAALKAGTVWINT-YNRFDPGSPFGGYKQSGFG--REMGREALDEYTEVKSV 449
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-481 |
2.40e-116 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 349.52 E-value: 2.40e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEV 107
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 108 QRGIECVEFAAGAPtlmmgkqLPDIA----TGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERT 183
Cdd:cd07106 81 GGAVAWLRYTASLD-------LPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 184 PLLAARLVELFEEAgLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLN 263
Cdd:cd07106 154 PLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 264 DADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIES 343
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 344 GVEEGARLVRDGredHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSG 423
Cdd:cd07106 313 AKAKGAKVLAGG---EPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1750864354 424 ASVREFRENIESGMLGVN-VGVPAPMAffPFSGWKDSFYGdlHANGTDGVEFYTRKKMV 481
Cdd:cd07106 390 ERAEAVARRLEAGTVWINtHGALDPDA--PFGGHKQSGIG--VEFGIEGLKEYTQTQVI 444
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
25-466 |
6.47e-116 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 348.82 E-value: 6.47e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 25 TEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG--WSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNE 102
Cdd:cd07112 3 TFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 103 AR-GEVQRGIECVEFAAGAPTLMMGKQLPdIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSE 181
Cdd:cd07112 83 ALaVDVPSAANTFRWYAEAIDKVYGEVAP-TGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 182 RTPLLAARLVELFEEAGLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAEYVYK-KGTENLKRVQALAGAKNHS 259
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFgHTAGEALGLHMDVDALAFTGSTEVGRRFLEySGQSNLKRVWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 260 IVLNDA-DLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTL 338
Cdd:cd07112 242 IVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 339 SYIESGVEEGARLVRDGREDHAVkENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACI 418
Cdd:cd07112 322 GYIESGKAEGARLVAGGKRVLTE-TGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1750864354 419 YTDSGASVREFRENIESGMLGVNvGVPAPMAFFPFSGWKDSFYG---DLHA 466
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVN-CFDEGDITTPFGGFKQSGNGrdkSLHA 450
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
6-484 |
1.10e-115 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 348.95 E-value: 1.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 6 VKTVKNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFK---GWSKTAVPKRARILFKYQQLLV 82
Cdd:cd07141 4 IKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 83 DNWDELAKLVTLENGKSFNEAR-GEVQRGIECVEFAAGAPTLMMGKQLPdiATGIESGMYRY-PIGVIGGITPFNFPMMV 160
Cdd:cd07141 84 RDRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIP--MDGDFFTYTRHePVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 161 PCWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVY 239
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 240 KK-GTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNG 318
Cdd:cd07141 242 QAaGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 319 LEKDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVK 398
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGK---RHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 399 TLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNV-GVPAPMAffPFSGWKDSFYGdlHANGTDGVEFYTR 477
Cdd:cd07141 399 TIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCyNVVSPQA--PFGGYKMSGNG--RELGEYGLQEYTE 474
|
....*..
gi 1750864354 478 KKMVTAR 484
Cdd:cd07141 475 VKTVTIK 481
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
47-482 |
5.61e-114 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 342.59 E-value: 5.61e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 47 DVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMG 126
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 127 KQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTP-----LLAarlvELFEEAGLPK 201
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 202 GVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFG 280
Cdd:cd07104 157 GVLNVVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 281 SAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGREDha 360
Cdd:cd07104 237 HQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 361 vkenGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGV 440
Cdd:cd07104 315 ----GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1750864354 441 NVGVPAPMAFFPFSGWKDSFYGDLhaNGTDGVEFYTRKKMVT 482
Cdd:cd07104 391 NDQTVNDEPHVPFGGVKASGGGRF--GGPASLEEFTEWQWIT 430
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
28-482 |
1.04e-113 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 343.18 E-value: 1.04e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEV 107
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 108 QRGIECVEFAAG---APTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTP 184
Cdd:cd07110 81 DDVAGCFEYYADlaeQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 185 LLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLN 263
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGtGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 264 DADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIES 343
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 344 GVEEGARLVRDG-REDHAvkENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDS 422
Cdd:cd07110 321 GKEEGARLLCGGrRPAHL--EKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1750864354 423 GASVREFRENIESGMLGVNvgvpAPMAFFPFSGW---KDSFYG-DLhanGTDGVEFYTRKKMVT 482
Cdd:cd07110 399 AERCDRVAEALEAGIVWIN----CSQPCFPQAPWggyKRSGIGrEL---GEWGLDNYLEVKQIT 455
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
10-484 |
1.15e-112 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 340.70 E-value: 1.15e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 10 KNYIGGEWVDSSTSlTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTA-VPKRARILFKYQQLLVDNWDEL 88
Cdd:cd07082 3 KYLINGEWKESSGK-TIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMpLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 89 AKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLP-DI---ATGIESGMYRYPIGVIGGITPFNFPMMVP-CW 163
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPgDWfpgTKGKIAQVRREPLGVVLAIGPFNYPLNLTvSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 164 MFPLAIAcGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKG 242
Cdd:cd07082 162 LIPALIM-GNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 243 TenLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKD 322
Cdd:cd07082 241 P--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 323 VFLGPVIRENHKERTLSYIESGVEEGARLVRDGRedhavKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEE 402
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG-----REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 403 AIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSfygdlhANGTDGV----EFYTRK 478
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDS------GIGTQGIgdalRSMTRR 467
|
....*.
gi 1750864354 479 KMVTAR 484
Cdd:cd07082 468 KGIVIN 473
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
27-462 |
1.57e-112 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 339.69 E-value: 1.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 27 PVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGE 106
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 107 VQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLL 186
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 187 AARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDA 265
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 266 DLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGV 345
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 346 EEGARLVRDGredhavKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGAS 425
Cdd:cd07150 322 AKGAKLLTGG------KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 1750864354 426 VREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYG 462
Cdd:cd07150 396 AFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFG 432
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
10-481 |
1.91e-110 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 335.70 E-value: 1.91e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 10 KNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELA 89
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNEAR-GEVQRGIECVEFAAG-APTLMmGKQLPDIATgieSGMY--RYPIGVIGGITPFNFPMMVPCWMF 165
Cdd:PRK13252 88 ALETLDTGKPIQETSvVDIVTGADVLEYYAGlAPALE-GEQIPLRGG---SFVYtrREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 166 PLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTEN 245
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 246 LKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFL 325
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 326 GPVIRENHKERTLSYIESGVEEGARLVRDG-REDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAI 404
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGeRLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1750864354 405 DVANNSRFANGACIYTDSGASVREFRENIESGMLGVNV--GVPAPMaffPFSGWKDSFYGdlHANGTDGVEFYTRKKMV 481
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEM---PVGGYKQSGIG--RENGIATLEHYTQIKSV 477
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
31-482 |
4.07e-110 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 333.54 E-value: 4.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 31 PATGEVIAEVPLSTKADVDQAVQAANEAF-KG-WSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQ 108
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFdKGpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 109 RGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAA 188
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 189 RLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADL 267
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 268 NVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGVEE 347
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 348 GARLVRDGreDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVR 427
Cdd:cd07118 324 GATLLLGG--ERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1750864354 428 EFRENIESGMLGVNV---GVPApmafFPFSGWKDSFYGdlHANGTDGVEFYTRKKMVT 482
Cdd:cd07118 402 TVARRIRAGTVWVNTfldGSPE----LPFGGFKQSGIG--RELGRYGVEEYTELKTVH 453
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
12-485 |
2.05e-109 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 333.83 E-value: 2.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTepVYNPA-TGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAK 90
Cdd:PRK03137 40 IIGGERITTEDKIV--SINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 91 LVTLENGKSFNEARGEVQRGIECVEF--------AAGAPTLmmgkQLPDiatgiESGMYRY-PIGVIGGITPFNFPMMVP 161
Cdd:PRK03137 118 WLVKEAGKPWAEADADTAEAIDFLEYyarqmlklADGKPVE----SRPG-----EHNRYFYiPLGVGVVISPWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 162 CWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVY- 239
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYe 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 240 -----KKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIV 314
Cdd:PRK03137 269 raakvQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 315 IGNGLEKDvFLGPVIRENHKERTLSYIESGVEEGaRLVRDGREDhavKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSI 394
Cdd:PRK03137 349 VGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGD---DSKGYFIQPTIFADVDPKARIMQEEIFGPVVAF 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 395 VRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPM-AFFPFSGWKDSfyG-DLHANGTDGV 472
Cdd:PRK03137 424 IKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIvGYHPFGGFNMS--GtDSKAGGPDYL 501
|
490
....*....|...
gi 1750864354 473 EFYTRKKMVTARY 485
Cdd:PRK03137 502 LLFLQAKTVSEMF 514
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
28-483 |
5.07e-109 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 330.74 E-value: 5.07e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVP-KRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGE 106
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPaERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 107 VQRGIECVEFAAGAPTLMMGKQLPdIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLL 186
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 187 AARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDA 265
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 266 DLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEkDVFLGPVIRENHKERTLSYIESGV 345
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 346 EEGARLVRDGREDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGAS 425
Cdd:cd07109 319 ARGARIVAGGRIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1750864354 426 VREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGdlHANGTDGVEFYTRKKMVTA 483
Cdd:cd07109 399 ALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHG--REKGLEALYNYTQTKTVAV 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
15-482 |
7.04e-108 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 328.49 E-value: 7.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 15 GEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTL 94
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 95 ENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNT 174
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 175 FVLKPSERTP----LLAARlveLFEEAGLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRV 249
Cdd:cd07151 161 VVLKPASDTPitggLLLAK---IFEEAGLPKGVLNVVVGAgSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 250 QALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVI 329
Cdd:cd07151 238 ALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 330 RENHKERTLSYIESGVEEGARLVRDGredhavKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANN 409
Cdd:cd07151 318 NESQVDGLLDKIEQAVEEGATLLVGG------EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1750864354 410 SRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGDLhaNGTDGVEFYTRKKMVT 482
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRF--NGEWALEEFTTDKWIS 462
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
6-481 |
1.76e-107 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 327.91 E-value: 1.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 6 VKTVKNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFK--GWSKTAVPKRARILFKYQQLLVD 83
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 84 NWDELAKLVTLENGKSFNEAR-GEVQRGIECVEFAAGAPTLMMGKQLPdiATGIESGMYRY-PIGVIGGITPFNFPMMVP 161
Cdd:cd07142 81 HADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLP--ADGPHHVYTLHePIGVVGQIIPWNFPLLMF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 162 CWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNG-LLEHKLVKAISFVGSQPVAEYVYK 240
Cdd:cd07142 159 AWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 241 KGTE-NLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGL 319
Cdd:cd07142 239 LAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 320 EKDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKT 399
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGD---RIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 400 LEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNV-GVPAPMAffPFSGWKDSFYGdlHANGTDGVEFYTRK 478
Cdd:cd07142 396 VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCyDVFDASI--PFGGYKMSGIG--REKGIYALNNYLQV 471
|
...
gi 1750864354 479 KMV 481
Cdd:cd07142 472 KAV 474
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
12-485 |
9.66e-107 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 325.94 E-value: 9.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG-WSKTAVPKRARILFKYQQLLVDNWDELAK 90
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 91 LVTLENGKSFNEARG-EVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMY-----RYPIGVIGGITPFNFPMMVPCWM 164
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLAPSIPSMQGERYtaftrREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 165 FPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTE 244
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 245 NLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVF 324
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 325 LGPVIRENHKERTLSYIESGVEEGARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAI 404
Cdd:cd07113 323 FGPLANQPHFDKVCSYLDDARAEGDEIVRGGE---ALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 405 DVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGV---PApmafFPFSGWKDSFYGdlHANGTDGVEFYTRKKMV 481
Cdd:cd07113 400 QLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTfldPA----VPFGGMKQSGIG--REFGSAFIDDYTELKSV 473
|
....
gi 1750864354 482 TARY 485
Cdd:cd07113 474 MIRY 477
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
27-459 |
1.46e-106 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 324.69 E-value: 1.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 27 PVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGE 106
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 107 VQRGIECVEFAAGAPTLMMGKQLP-DIATGIESGM---YRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSER 182
Cdd:cd07145 82 VERTIRLFKLAAEEAKVLRGETIPvDAYEYNERRIaftVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 183 TPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIV 261
Cdd:cd07145 162 TPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 262 LNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYI 341
Cdd:cd07145 242 LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 342 ESGVEEGARLVRDGRedhavKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTD 421
Cdd:cd07145 322 NDAVEKGGKILYGGK-----RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 1750864354 422 SGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDS 459
Cdd:cd07145 397 DINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKS 434
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-482 |
2.09e-106 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 323.89 E-value: 2.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEAR-GE 106
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 107 VQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLL 186
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 187 AARLVELFEEaGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDA 265
Cdd:cd07092 161 TLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 266 DLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIEsGV 345
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE-RA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 346 EEGARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYT-DSGA 424
Cdd:cd07092 319 PAHARVLTGGR---RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTrDVGR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1750864354 425 SVREFREnIESGMLGVNVGVPaPMAFFPFSGWKDSFYG-DLhanGTDGVEFYTRKKMVT 482
Cdd:cd07092 396 AMRLSAR-LDFGTVWVNTHIP-LAAEMPHGGFKQSGYGkDL---SIYALEDYTRIKHVM 449
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
10-459 |
3.43e-106 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 324.68 E-value: 3.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 10 KNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELA 89
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNEARG-EVQRGIECVEFAAGAPTLMMGkQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLA 168
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEG-SLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 169 IACGNTFVLKPSERTPLLAARLVELFEEAgLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLK 247
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 248 RVQALAGAKNHSIVLNDADLNVAT--KQIIGAAFGSA---GERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKD 322
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAMDADDDfdDKAEEGQLGFAfnqGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 323 VFLGPVIRENHKERTLSYIESGVEEGARLVRDGREDH-AVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLE 401
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1750864354 402 EAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPmAFFPFSGWKDS 459
Cdd:cd07559 400 EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYP-AHAPFGGYKKS 456
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-479 |
5.87e-106 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 323.04 E-value: 5.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWS-KTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKS-FNEARG 105
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPvMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 106 EVQRGIECVEFAAG-APTLMMGKQLPDIATGIESGM---YRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSE 181
Cdd:cd07089 81 QVDGPIGHLRYFADlADSFPWEFDLPVPALRGGPGRrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 182 RTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLL-EHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSI 260
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALtTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 261 VLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSY 340
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 341 IESGVEEGARLVRDG-REDHAvkENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIY 419
Cdd:cd07089 321 IARGRDEGARLVTGGgRPAGL--DKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 420 TDSGASVREFRENIESGMLGVNVGVpAPMAFFPFSGWKDSFYGdlHANGTDGVEFYTRKK 479
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGG-GYGPDAPFGGYKQSGLG--RENGIEGLEEFLETK 455
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-481 |
5.96e-105 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 321.40 E-value: 5.96e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVP--KRARILFKYQQLLVDNWDELA 89
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSgsKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNE-ARGEVQRGIECVEFAAGAPTLMMGKQlpdIATGIESGMY--RYPIGVIGGITPFNFPMMVPCWMFP 166
Cdd:cd07143 90 SIEALDNGKTFGTaKRVDVQASADTFRYYGGWADKIHGQV---IETDIKKLTYtrHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 167 LAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTE- 244
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKs 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 245 NLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVF 324
Cdd:cd07143 247 NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 325 LGPVIRENHKERTLSYIESGVEEGARLVRDGrEDHAVKenGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAI 404
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGG-KRHGNE--GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1750864354 405 DVANNSRFANGACIYTDSGASVREFRENIESGMLGVN-VGVPAPMAffPFSGWKDSFYGdlHANGTDGVEFYTRKKMV 481
Cdd:cd07143 404 KRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV--PFGGYKQSGIG--RELGEYALENYTQIKAV 477
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-481 |
3.51e-104 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 319.16 E-value: 3.51e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 8 TVKNYIGGEWVDSSTSlTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDE 87
Cdd:PRK13473 2 QTKLLINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 88 LAKLVTLENGKSFNEARG-EVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFP 166
Cdd:PRK13473 81 FARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 167 LAIACGNTFVLKPSERTPLLAARLVELFEEAgLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTEN 245
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 246 LKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFL 325
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 326 GPVIRENHKERTLSYIESGVEEG-ARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAI 404
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGhIRVVTGGE---APDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 405 DVANNSRFANGACIYT-DSGASVREFREnIESGMLGVNVGVP--APMaffPFSGWKDSFYG-DLHAngtDGVEFYTRKKM 480
Cdd:PRK13473 397 RWANDSDYGLASSVWTrDVGRAHRVSAR-LQYGCTWVNTHFMlvSEM---PHGGQKQSGYGkDMSL---YGLEDYTVVRH 469
|
.
gi 1750864354 481 V 481
Cdd:PRK13473 470 V 470
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-485 |
2.05e-102 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 315.52 E-value: 2.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG-----WSKTAVPKRARILFKYQQLLVDNWD 86
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 87 ELAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIES---GMYRYPIGVIGGITPFNFPMMVPCW 163
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETfkgYVLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 164 MFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAEYVYKKG 242
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTATGRKIMTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 243 TENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKD 322
Cdd:PLN02467 251 AQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 323 VFLGPVIRENHKERTLSYIESGVEEGARLVRDGREDHAVKEnGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEE 402
Cdd:PLN02467 331 CRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKK-GFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 403 AIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPApMAFFPFSGWKDSFYG-DLhanGTDGVEFYTRKKMV 481
Cdd:PLN02467 410 AIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPC-FCQAPWGGIKRSGFGrEL---GEWGLENYLSVKQV 485
|
....
gi 1750864354 482 TaRY 485
Cdd:PLN02467 486 T-KY 488
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-462 |
4.22e-101 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 311.31 E-value: 4.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEARG-EVQRGIECVEFAAGAPTLMMGkQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIA 170
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEG-SANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 171 CGNTFVLKPSERTPLLAARLVELFEEAgLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRV 249
Cdd:cd07117 163 AGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 250 QALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVI 329
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 330 RENHKERTLSYIESGVEEGARLVRDGR---EDHAVKenGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDV 406
Cdd:cd07117 322 NKDQLDKILSYVDIAKEEGAKILTGGHrltENGLDK--GFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1750864354 407 ANNSRFANGACIYT-DSGASVREFREnIESGMLGVNVGVPAPmAFFPFSGWKDSFYG 462
Cdd:cd07117 400 ANDSEYGLGGGVFTkDINRALRVARA-VETGRVWVNTYNQIP-AGAPFGGYKKSGIG 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-482 |
7.39e-100 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 307.96 E-value: 7.39e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG--WSKTAVPKRARILFKYQQLLVDNWDELA 89
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENG---KSFneARGEVQRGIECVE-FAAGAPTLMMGKQLPDIATGieSGMYRY-PIGVIGGITPFNFPMMVPCWM 164
Cdd:cd07139 82 RLWTAENGmpiSWS--RRAQGPGPAALLRyYAALARDFPFEERRPGSGGG--HVLVRRePVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 165 FPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTE 244
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 245 NLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVF 324
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 325 LGPVIRENHKERTLSYIESGVEEGARLVRDG-REDHAvkENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEA 403
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGgRPAGL--DRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 404 IDVANNSRFANGACIYT-DSGASVREFREnIESGMLGVNVGVPAPMAffPFSGWKDSFYGdlHANGTDGVEFYTRKKMVT 482
Cdd:cd07139 396 VRIANDSDYGLSGSVWTaDVERGLAVARR-IRTGTVGVNGFRLDFGA--PFGGFKQSGIG--REGGPEGLDAYLETKSIY 470
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
34-482 |
3.88e-98 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 302.68 E-value: 3.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 34 GEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQRGIEC 113
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 114 VEFAAGAPTLMMGKQLPDiATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTP----LLAAR 189
Cdd:cd07152 81 LHEAAGLPTQPQGEILPS-APGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsggVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 190 LvelFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNV 269
Cdd:cd07152 160 L---FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 270 ATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGVEEGA 349
Cdd:cd07152 237 AASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 350 RLVRDGREDhavkenGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREF 429
Cdd:cd07152 317 RLEAGGTYD------GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1750864354 430 RENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGDLHAnGTDGVEFYTRKKMVT 482
Cdd:cd07152 391 ADRLRTGMLHINDQTVNDEPHNPFGGMGASGNGSRFG-GPANWEEFTQWQWVT 442
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
28-485 |
1.73e-97 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 301.22 E-value: 1.73e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEV 107
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 108 QRGIECVEFAAGAPTLMMGKQLPdiaTGIESGMY--RYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPL 185
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIP---VGGRNLHYtlREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 186 LAARLVELFEEAgLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLND 264
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 265 ADLNVATKQII-GAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIES 343
Cdd:cd07107 237 ADPEAAADAAVaGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 344 GVEEGARLVRDG-REDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYT-D 421
Cdd:cd07107 317 AKREGARLVTGGgRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTnD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1750864354 422 SGASVREFREnIESGMLGVNvGVPAPMAFFPFSGWKDSFYGDLHanGTDGVEFYTRKKMVTARY 485
Cdd:cd07107 397 ISQAHRTARR-VEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREE--CLEELLSYTQEKNVNVRL 456
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
27-481 |
1.75e-97 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 301.09 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 27 PVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGE 106
Cdd:cd07147 2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 107 VQRGIECVEFAAGAPTLMMGKQLP-DIATGIE--SGMY-RYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSER 182
Cdd:cd07147 82 VARAIDTFRIAAEEATRIYGEVLPlDISARGEgrQGLVrRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 183 TPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAeyvYK-KGTENLKRVQALAGAKNHSIV 261
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVG---WDlKARAGKKKVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 262 LNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYI 341
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 342 ESGVEEGARLVRDGREDHAVKEngyfvgPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYT- 420
Cdd:cd07147 319 NEAVDAGAKLLTGGKRDGALLE------PTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTr 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 421 DSGASVREFrENIESGmlGVNVG-VPA----PMaffPFSGWKDSfygdlhANGTDGVEF----YTRKKMV 481
Cdd:cd07147 393 DLEKALRAW-DELEVG--GVVINdVPTfrvdHM---PYGGVKDS------GIGREGVRYaieeMTEPRLL 450
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
47-482 |
3.23e-97 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 299.88 E-value: 3.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 47 DVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMG 126
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 127 KQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNI 206
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 207 VN----GAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSA 282
Cdd:cd07105 161 VThspeDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 283 GERCMAASVVTVQEDVADELISRLVQESNNIVIGnglekDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGREDHAvk 362
Cdd:cd07105 241 GQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADES-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 363 ENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNV 442
Cdd:cd07105 314 PSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1750864354 443 GVPAPMAFFPFSGWKDSFYGDLhaNGTDGVEFYTRKKMVT 482
Cdd:cd07105 394 MTVHDEPTLPHGGVKSSGYGRF--NGKWGIDEFTETKWIT 431
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
28-482 |
1.03e-96 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 299.35 E-value: 1.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEV 107
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 108 QRGIECVEFAAGAPTLMMGKQLP-DIATGIESGM---YRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERT 183
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEIPlDATQGSDNRLawtIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 184 PLLAARLVELFEEAGLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGteNLKRVQALAGAKNHSIVL 262
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEALRANA--GGKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 263 NDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIE 342
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 343 SGVEEGARLVRDGREDHAVkengyfVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDS 422
Cdd:cd07094 321 EAVEAGARLLCGGERDGAL------FKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1750864354 423 GASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYgdlhanGTDGVEF----YTRKKMVT 482
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGV------GREGVPYameeMTEEKTVV 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
28-482 |
1.70e-95 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 296.19 E-value: 1.70e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSF-NEARGE 106
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 107 VQRGIECVEFAAGAPTLMMGKQLPdIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLL 186
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 187 AARLVELFEEAgLPKGVLNIVNGAHDVVN-GLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDA 265
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGaALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 266 DLNVATKQII-GAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESG 344
Cdd:cd07108 239 DLDDAVDGAIaGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 345 VEE-GARLVRDGREDHAVK-ENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYT-D 421
Cdd:cd07108 319 LSTsGATVLRGGPLPGEGPlADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTrD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1750864354 422 SGASVREFREnIESGMLGVNVGVpAPMAFFPFSGWKDSFYGDLHAngTDG-VEFYTRKKMVT 482
Cdd:cd07108 399 LGRALRAAHA-LEAGWVQVNQGG-GQQPGQSYGGFKQSGLGREAS--LEGmLEHFTQKKTVN 456
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
12-459 |
2.85e-95 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 295.75 E-value: 2.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTsltEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:NF040648 2 FINGKWIDRED---IDVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPdiatgIESGM---YRYPIGVIGGITPFNFPMMVPCWMFPLA 168
Cdd:NF040648 79 ITIDAGKPIKQSIIEVDRSIETFKLAAFYAKEIRGETIP-----SDAGLiftKKEPLGVVGAITPFNYPLNLAAHKIAPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 169 IACGNTFVLKPSERTPLLAARLVELFEEA----GLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGt 243
Cdd:NF040648 154 IATGNSVVLHPSSKAPLAAIELAKIIEKVlkkmNIPLGVFNLVTGYGEVVgDEIVKNEKVNKISFTGSVEVGESISKKA- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 244 eNLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDV 323
Cdd:NF040648 233 -GMKKITLELGGNNPLIVLKDADIEKAVESAVKGSFLNSGQVCISVGRVIVEEEIADEFIKKLVEETKKLKVGNPLDEKT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 324 FLGPVIRENHKERTLSYIESGVEEGARLVRDGREDhavkenGYFVGPTIFDnVTQEMKIWQDEIFAPVLSIVRVKTLEEA 403
Cdd:NF040648 312 DIGPLITEEAAIRVENLVNEAIEEGAKLLCGGNRE------GSLFYPTVLD-VDEDNILVKVETFGPVLPIIRVKDIDEA 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1750864354 404 IDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDS 459
Cdd:NF040648 385 IEIANNTKYGLQAGVFTNDINKALKFADELEYGGVIINKSSTFRTDNMPFGGFKKS 440
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
29-483 |
9.89e-95 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 294.13 E-value: 9.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 29 YNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQ 108
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 109 RGIECVEFAAG-APTLM------MGKQLPDIATGIEsgmYRyPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSE 181
Cdd:cd07099 81 LALEAIDWAARnAPRVLaprkvpTGLLMPNKKATVE---YR-PYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 182 RTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKlVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIV 261
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 262 LNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYI 341
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 342 ESGVEEGARLVRDGREdhaVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTD 421
Cdd:cd07099 316 DDAVAKGAKALTGGAR---SNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1750864354 422 SGASVREFRENIESGMLGVN-VGVPAPMAFFPFSGWKDSFYGDLHanGTDGVEFYTRKKMVTA 483
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVKDSGGGRRH--GAEGLREFCRPKAIAR 453
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
12-485 |
2.26e-94 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 294.40 E-value: 2.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG--WSKTAVPKRARILFKYQQLLVDNWDELA 89
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNEA-RGEVQRGIECVEFAAGAPTLMMGKQLP-DIATGIESGMY--RYPIGVIGGITPFNFPMMVPCWMF 165
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPiNQARPNRNLTLtkREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 166 PLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKK-GT 243
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIMKScAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 244 ENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDV 323
Cdd:cd07140 249 SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRST 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 324 FLGPVIRENHKERTLSYIESGVEEGARLVRDGREdhaVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKT--LE 401
Cdd:cd07140 329 DHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQ---VDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 402 EAIDVANNSRFANGACIYT-DSGASVReFRENIESGMLGVNVGVPAPMAfFPFSGWKDSFYG-DLhanGTDGVEFYTRKK 479
Cdd:cd07140 406 GVLQRANDTEYGLASGVFTkDINKALY-VSDKLEAGTVFVNTYNKTDVA-APFGGFKQSGFGkDL---GEEALNEYLKTK 480
|
....*.
gi 1750864354 480 MVTARY 485
Cdd:cd07140 481 TVTIEY 486
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
5-485 |
2.79e-94 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 294.42 E-value: 2.79e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 5 TVKTVKNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG--WSKTAVPKRARILFKYQQLLV 82
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 83 DNWDELAKLVTLENGKSFNEARG-EVQRGIECVEFAAGAPTLMMGKQLpDIATGIESGMYRYPIGVIGGITPFNFPMMVP 161
Cdd:PLN02766 97 EHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 162 CWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLL-EHKLVKAISFVGSQPVAEYVYK 240
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIaSHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 241 K-GTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGL 319
Cdd:PLN02766 256 AaATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 320 EKDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKT 399
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGK---PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 400 LEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNvgvpAPMAF---FPFSGWKDSFYG-DLhanGTDGVEFY 475
Cdd:PLN02766 413 VEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN----CYFAFdpdCPFGGYKMSGFGrDQ---GMDALDKY 485
|
490
....*....|.
gi 1750864354 476 TR-KKMVTARY 485
Cdd:PLN02766 486 LQvKSVVTPLY 496
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
12-483 |
3.14e-91 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 285.83 E-value: 3.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEAR-GEVQRGIECVEFAAGAPTLMmgkqlpdiatgiESGMYRY-PIGVIGGITPFNFPMMVPCWMFPLAI 169
Cdd:cd07111 105 ESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLL------------DTELAGWkPVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 170 ACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRV 249
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 250 QALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVI 329
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 330 RENHKERTLSYIESGVEEGARLVrdgREDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANN 409
Cdd:cd07111 333 DPAQLKRIRELVEEGRAEGADVF---QPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1750864354 410 SRFANGACIYTDSGASVREFRENIESGMLGVNV-GVPAPMAffPFSGWKDSFYGdlHANGTDGVEFYTRKKMVTA 483
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGhNLFDAAA--GFGGYRESGFG--REGGKEGLYEYLRPSWEPA 480
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
48-462 |
4.95e-91 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 283.58 E-value: 4.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 48 VDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQRGIECVEF-AAGAPTLMMG 126
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 127 KQLPdiATGIESGMYRYPIGVIGGITPFNFPM------MVPcwmfplAIACGNTFVLKPSERTPLLAARLVELFEEAGLP 200
Cdd:cd07100 81 EPIE--TDAGKAYVRYEPLGVVLGIMPWNFPFwqvfrfAAP------NLMAGNTVLLKHASNVPGCALAIEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 201 KGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKR-VQALAGaknhS---IVLNDADLNVATKQIIG 276
Cdd:cd07100 153 EGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKsVLELGG----SdpfIVLDDADLDKAVKTAVK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 277 AAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGr 356
Cdd:cd07100 229 GRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 357 edHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESG 436
Cdd:cd07100 308 --KRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAG 385
|
410 420
....*....|....*....|....*.
gi 1750864354 437 MLGVNvGVPAPMAFFPFSGWKDSFYG 462
Cdd:cd07100 386 MVFIN-GMVKSDPRLPFGGVKRSGYG 410
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
28-482 |
6.10e-91 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 284.25 E-value: 6.10e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAAneaFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEV 107
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA---ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 108 QRGIECVEFAAGAPTLMMGKQLP-DIATGIESGM---YRYPIGVIGGITPFNFPM-MVPCWMFPlAIACGNTFVLKPSER 182
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFScDLTANGKARKiftLREPLGVVLAITPFNHPLnQVAHKIAP-AIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 183 TPLLAARLVELFEEAGLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAEYV-----YKKGTENLkrvqalaGAK 256
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIaatagYKRQLLEL-------GGN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 257 NHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKER 336
Cdd:cd07146 232 DPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 337 TLSYIESGVEEGARLVRDGREDhavkenGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGA 416
Cdd:cd07146 312 IENRVEEAIAQGARVLLGNQRQ------GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSS 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 417 CIYTDSGASVREFRENIESGMLGVNVGVPAPMAFFPFSGWKDSFYGdlhanGTDGV----EFYTRKKMVT 482
Cdd:cd07146 386 GVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSELSPFGGVKDSGLG-----GKEGVreamKEMTNVKTYS 450
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
29-482 |
5.14e-90 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 281.92 E-value: 5.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 29 YNPATGEVIAEVPLSTKADVDQAVQAANEAFKG--WSKTAvPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGE 106
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 107 VQRGIECVEFAAGAPTLMMGKQLpDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLL 186
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMI-EPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 187 AARLVELFEEA-GLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLND 264
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 265 ADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESG 344
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 345 VEEGAR-LVRDGREDHAVKeNGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSG 423
Cdd:cd07120 320 IAAGAEvVLRGGPVTEGLA-KGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1750864354 424 AsvREFR--ENIESGMLGVNVGVpAPMAFFPFSGWKDSFYGDLHanGTDGVEFYTRKKMVT 482
Cdd:cd07120 399 A--RAMRvaRAIRAGTVWINDWN-KLFAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIY 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
6-481 |
3.55e-89 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 282.47 E-value: 3.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 6 VKTVKNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG--WSKTAVPKRARILFKYQQLLVD 83
Cdd:PLN02466 55 VSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 84 NWDELAKLVTLENGKSFNEARG-EVQRGIECVEFAAGAPTLMMGKQLPdiATGIES-GMYRYPIGVIGGITPFNFPMMVP 161
Cdd:PLN02466 135 HNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVP--ADGPHHvQTLHEPIGVAGQIIPWNFPLLMF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 162 CWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLL-EHKLVKAISFVGSQPVAEYVYK 240
Cdd:PLN02466 213 AWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALaSHMDVDKLAFTGSTDTGKIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 241 KGTE-NLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGL 319
Cdd:PLN02466 293 LAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPF 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 320 EKDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGREdhaVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKT 399
Cdd:PLN02466 373 KKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDR---FGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 400 LEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVgVPAPMAFFPFSGWKDSFYGdlHANGTDGVEFYTRKK 479
Cdd:PLN02466 450 LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNC-FDVFDAAIPFGGYKMSGIG--REKGIYSLNNYLQVK 526
|
..
gi 1750864354 480 MV 481
Cdd:PLN02466 527 AV 528
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
12-466 |
2.12e-88 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 279.09 E-value: 2.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKG--WSKTAVPKRARILFKYQQLLVDNWDELA 89
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNEA-RGEVQRGIECVEFAAGAPTLMMGKQLPdiATGIESGMY-RYPIGVIGGITPFNFPMMVPCWMFPL 167
Cdd:PRK09847 103 LLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVAT--TSSHELAMIvREPVGVIAAIVPWNFPLLLTCWKLGP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 168 AIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYK-KGTEN 245
Cdd:PRK09847 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKdAGDSN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 246 LKRVQALAGAKNHSIVLNDA-DLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVF 324
Cdd:PRK09847 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 325 LGPVIRENHKERTLSYIESGVEEGARLVrDGRED-HAVkengyFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEA 403
Cdd:PRK09847 341 MGTLIDCAHADSVHSFIREGESKGQLLL-DGRNAgLAA-----AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1750864354 404 IDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAfFPFSGWKDSFYG---DLHA 466
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT-VPFGGYKQSGNGrdkSLHA 479
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
18-476 |
1.92e-87 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 277.53 E-value: 1.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 18 VDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENG 97
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 98 KSFNEARGEVQR-GIECVEFAAGAPTLMMGKQ----LPDIATGIEsgmYRYPIGVIGGITPFNFPM------MVPcwmfp 166
Cdd:PRK09407 106 KARRHAFEEVLDvALTARYYARRAPKLLAPRRragaLPVLTKTTE---LRQPKGVVGVISPWNYPLtlavsdAIP----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 167 lAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNG-LLEHklVKAISFVGSQPVAEYVYKKGTEN 245
Cdd:PRK09407 178 -ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTaLVDN--ADYLMFTGSTATGRVLAEQAGRR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 246 LKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFL 325
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 326 GPVIRENHKERTLSYIESGVEEGARLVRDGRedhAVKENG-YFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAI 404
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGK---ARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAV 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1750864354 405 DVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVG-------VPAPMAffpfsGWKDSFYGDLHanGTDGVEFYT 476
Cdd:PRK09407 412 ERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGyaaawgsVDAPMG-----GMKDSGLGRRH--GAEGLLKYT 483
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
12-462 |
6.10e-86 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 272.55 E-value: 6.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIAC 171
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 172 GNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQ 250
Cdd:PRK11241 174 GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGsAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 251 ALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIR 330
Cdd:PRK11241 254 LELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 331 ENHKERTLSYIESGVEEGARLVRDGREdHAVkeNGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNS 410
Cdd:PRK11241 334 EKAVAKVEEHIADALEKGARVVCGGKA-HEL--GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDT 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1750864354 411 RFANGACIYTDSGASVREFRENIESGMLGVNVGVPApMAFFPFSGWKDSFYG 462
Cdd:PRK11241 411 EFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIIS-NEVAPFGGIKASGLG 461
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
12-410 |
1.65e-85 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 271.00 E-value: 1.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTepVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:cd07130 2 VYDGEWGGGGGVVT--SISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGieSGMYR--YPIGVIGGITPFNFPMMVPCWMFPLAI 169
Cdd:cd07130 80 VSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPG--HRMMEqwNPLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 170 ACGNTFVLKPSERTPLLAA---RLV-ELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTEN 245
Cdd:cd07130 158 VCGNVVVWKPSPTTPLTAIavtKIVaRVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 246 LKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFL 325
Cdd:cd07130 238 FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 326 GPVIRENHKERTLSYIESGVEEGARLVRDGRedhAVKENGYFVGPTIFDnVTQEMKIWQDEIFAPVLSIVRVKTLEEAID 405
Cdd:cd07130 318 GPLHTKAAVDNYLAAIEEAKSQGGTVLFGGK---VIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIA 393
|
....*
gi 1750864354 406 VaNNS 410
Cdd:cd07130 394 W-NNE 397
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
29-479 |
1.36e-84 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 267.96 E-value: 1.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 29 YNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQ 108
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 109 RGIECVEF----AAGAptlmmgkqLPDIATGIESGMYRY----PIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPS 180
Cdd:cd07102 81 GMLERARYmisiAEEA--------LADIRVPEKDGFERYirrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 181 ERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSI 260
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 261 VLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSY 340
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 341 IESGVEEGARLVRDGREDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYT 420
Cdd:cd07102 313 IADAIAKGARALIDGALFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1750864354 421 DSGASVREFRENIESGMLGVNVGV---PApmafFPFSGWKDSFYGdlHANGTDGVEFYTRKK 479
Cdd:cd07102 393 KDIARAEALGEQLETGTVFMNRCDyldPA----LAWTGVKDSGRG--VTLSRLGYDQLTRPK 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
31-476 |
1.38e-83 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 265.33 E-value: 1.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 31 PATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEV-QR 109
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVlDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 110 GIECVEFAAGAPTLMMGKQ----LPDIATGIEsgmYRYPIGVIGGITPFNFPM------MVPcwmfplAIACGNTFVLKP 179
Cdd:cd07101 83 AIVARYYARRAERLLKPRRrrgaIPVLTRTTV---NRRPKGVVGVISPWNYPLtlavsdAIP------ALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 180 SERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNG-LLEHklVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNH 258
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGaIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 259 SIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTL 338
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 339 SYIESGVEEGARLVRDGRedhAVKENG-YFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGAC 417
Cdd:cd07101 312 AHVDDAVAKGATVLAGGR---ARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1750864354 418 IYTDSGASVREFRENIESGMLGVNVG-------VPAPMAffpfsGWKDSFYGdlHANGTDGVEFYT 476
Cdd:cd07101 389 VWTRDGARGRRIAARLRAGTVNVNEGyaaawasIDAPMG-----GMKDSGLG--RRHGAEGLLKYT 447
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
12-485 |
3.95e-82 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 262.90 E-value: 3.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTepVYNP-ATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAK 90
Cdd:cd07083 22 VIGGEWVDTKERMV--SVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 91 LVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQ--LPDIATGIESGMYRyPIGVIGGITPFNFPMMVPCWMFPLA 168
Cdd:cd07083 100 TLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAveVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 169 IACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGTENL- 246
Cdd:cd07083 179 VAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLAp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 247 -----KRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEK 321
Cdd:cd07083 259 gqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 322 DVFLGPVIRENHKERTLSYIESGVEEGaRLVRDGREDHAvkeNGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKT-- 399
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEG---EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDdd 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 400 LEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVN-------VGVPapmaffPFSGWKDSFYGDlHANGTDGV 472
Cdd:cd07083 415 FAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkitgalVGVQ------PFGGFKLSGTNA-KTGGPHYL 487
|
490
....*....|...
gi 1750864354 473 EFYTRKKMVTARY 485
Cdd:cd07083 488 RRFLEMKAVAERF 500
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
47-459 |
2.81e-81 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 258.74 E-value: 2.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 47 DVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMG 126
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 127 KQLPDIATGIESGMYRyPIGVIGGITPFNFPM------MVPcwmfplAIACGNTFVLKPSERTPLLAARLVELFEEAGLP 200
Cdd:cd07095 81 ERATPMAQGRAVLRHR-PHGVMAVFGPFNFPGhlpnghIVP------ALLAGNTVVFKPSELTPAVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 201 KGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALA-GAKNHSIVLNDADLNVATKQIIGAAF 279
Cdd:cd07095 154 PGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEmGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 280 GSAGERCMAASVVTVQED-VADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGRed 358
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 359 hAVKENGYFVGPTIFDnVTqEMKIWQD-EIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGM 437
Cdd:cd07095 312 -RLVAGTAFLSPGIID-VT-DAADVPDeEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGI 388
|
410 420
....*....|....*....|....*
gi 1750864354 438 LGVN---VGVPAPMaffPFSGWKDS 459
Cdd:cd07095 389 VNWNrptTGASSTA---PFGGVGLS 410
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
25-462 |
6.15e-81 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 260.21 E-value: 6.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 25 TEPVYNPATGE-VIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEA 103
Cdd:cd07125 47 GAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 104 RGEVQRGIECVEF-AAGAPTLMMGKQLPDiATGiESGMYRY-PIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSE 181
Cdd:cd07125 127 DAEVREAIDFCRYyAAQARELFSDPELPG-PTG-ELNGLELhGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 182 RTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYK----KGTENLKRVqALAGAK 256
Cdd:cd07125 205 QTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINRalaeRDGPILPLI-AETGGK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 257 NHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKER 336
Cdd:cd07125 284 NAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 337 TLSYIESGVEEgARLVRDGREDhavKENGYFVGPTIFDNVtqemKIW--QDEIFAPVLSIVRVK--TLEEAIDVANNSRF 412
Cdd:cd07125 364 LRAHTELMRGE-AWLIAPAPLD---DGNGYFVAPGIIEIV----GIFdlTTEVFGPILHVIRFKaeDLDEAIEDINATGY 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1750864354 413 ANGACIYTDSGASVREFRENIESGMLGVN-------VGVPapmaffPFSGWKDSFYG 462
Cdd:cd07125 436 GLTLGIHSRDEREIEYWRERVEAGNLYINrnitgaiVGRQ------PFGGWGLSGTG 486
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
29-482 |
2.70e-78 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 251.84 E-value: 2.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 29 YNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEAR-GEV 107
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 108 QRGIECVEF--AAGAPTLMMGKQLPDIATGIESGMYRY-PIGVIGGITPFNFPM------MVPcwmfplAIACGNTFVLK 178
Cdd:cd07098 81 LVTCEKIRWtlKHGEKALRPESRPGGLLMFYKRARVEYePLGVVGAIVSWNYPFhnllgpIIA------ALFAGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 179 PSERTPLLAARLVELFEEA----GLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAG 254
Cdd:cd07098 155 VSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 255 AKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHK 334
Cdd:cd07098 235 GKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 335 ERTLSYIESGVEEGARLVRDG-REDHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFA 413
Cdd:cd07098 315 DRLEELVADAVEKGARLLAGGkRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYG 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 414 NGACIYTDSGASVREFRENIESGMLGVN-VGVPAPMAFFPFSGWKDSFYGDLhaNGTDGVEFYTRKKMVT 482
Cdd:cd07098 395 LGASVFGKDIKRARRIASQLETGMVAINdFGVNYYVQQLPFGGVKGSGFGRF--AGEEGLRGLCNPKSVT 462
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-462 |
5.27e-78 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 251.60 E-value: 5.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 11 NYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAK 90
Cdd:cd07116 3 NFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 91 LVTLENGKSFNEARG-EVQRGIECVEFAAGAPTLMMGKqLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAI 169
Cdd:cd07116 83 AETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGS-ISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 170 ACGNTFVLKPSERTPLLAARLVELFEEAgLPKGVLNIVNGAHDVVNG-LLEHKLVKAISFVGSQPVAEYVYKKGTENLKR 248
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKpLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 249 VQALAGAKNHSIVLND---ADLNVATKQIIGA---AFGSaGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKD 322
Cdd:cd07116 241 VTLELGGKSPNIFFADvmdADDAFFDKALEGFvmfALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 323 VFLGPVIRENHKERTLSYIESGVEEGARLVRDGREDH-AVKENGYFVGPTIFDNvTQEMKIWQDEIFAPVLSIVRVKTLE 401
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNElGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1750864354 402 EAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPmAFFPFSGWKDSFYG 462
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYP-AHAAFGGYKQSGIG 458
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
10-462 |
4.03e-70 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 231.57 E-value: 4.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 10 KNYIGGEWVDSSTSLTEPVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELA 89
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNEARGEVQRGIECVEFAA--GAPTLMMGKQL-PDIATGIESGMY----RYPIGVIGGITPFNFPMMVPC 162
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFLvSDSFPGNERNKYcltsKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 163 WMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQPVAEYVYKK 241
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGGDTGIAISKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 242 GTENLkrvQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGlEK 321
Cdd:PLN00412 257 GMVPL---QMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-ED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 322 DVFLGPVIRENHKERTLSYIESGVEEGARLVRDGREDhavkenGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLE 401
Cdd:PLN00412 333 DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRE------GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVE 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1750864354 402 EAIDVANNSRFANGACIYT-DSGASVReFRENIESGMLGVNvGVPA--PmAFFPFSGWKDSFYG 462
Cdd:PLN00412 407 EGIHHCNASNFGLQGCVFTrDINKAIL-ISDAMETGTVQIN-SAPArgP-DHFPFQGLKDSGIG 467
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
74-485 |
9.55e-70 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 228.08 E-value: 9.55e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 74 LFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITP 153
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 154 FNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQ 232
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 233 PVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNN 312
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 313 IVIGNGLEK-DVFLGPVIRENHKERTLSYIESGVEEGARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPV 391
Cdd:PRK10090 241 VQFGNPAERnDIAMGPLINAAALERVEQKVARAVEEGARVALGGK---AVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 392 LSIVRVKTLEEAIDVANNSRFANGACIYTDS-GASVREFREnIESGMLGVNVGVPAPMAFFpFSGWKDSFYGDlhANGTD 470
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNlNVAMKAIKG-LKFGETYINRENFEAMQGF-HAGWRKSGIGG--ADGKH 393
|
410
....*....|....*
gi 1750864354 471 GVEFYTRKKMVTARY 485
Cdd:PRK10090 394 GLHEYLQTQVVYLQS 408
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-441 |
1.74e-67 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 224.45 E-value: 1.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSS----TSLtepvyNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDE 87
Cdd:PRK09457 4 WINGDWIAGQgeafESR-----NPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 88 LAKLVTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRyPIGVIGGITPFNFP------MMVP 161
Cdd:PRK09457 79 LAEVIARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPghlpngHIVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 162 cwmfplAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKK 241
Cdd:PRK09457 158 ------ALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 242 GTENLKRVQALAGAKNHSIVLND-ADLNVATKQIIGAAFGSAGERCMAASVVTVQEDV-ADELISRLVQESNNIVIGN-G 318
Cdd:PRK09457 232 FAGQPEKILALEMGGNNPLVIDEvADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRwD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 319 LEKDVFLGPVIRENHKERTLSYIESGVEEGARLVrdgREDHAVKENGYFVGPTIFDnVTQEMKIWQDEIFAPVLSIVRVK 398
Cdd:PRK09457 312 AEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSL---LEMTQLQAGTGLLTPGIID-VTGVAELPDEEYFGPLLQVVRYD 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1750864354 399 TLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMlgVN 441
Cdd:PRK09457 388 DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VN 428
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
30-462 |
3.65e-67 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 222.81 E-value: 3.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 30 NPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQR 109
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 110 GIE-CVEFA-------AGAPTLMMGKQlpdiaTGIEsgmYRyPIGVIGGITPFNFPMmvpcWMF-----PLAIAcGNTFV 176
Cdd:PRK13968 93 SANlCDWYAehgpamlKAEPTLVENQQ-----AVIE---YR-PLGTILAIMPWNFPL----WQVmrgavPILLA-GNGYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 177 LKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAK 256
Cdd:PRK13968 159 LKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 257 NHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKER 336
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 337 TLSYIESGVEEGARLVRDGREdhaVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGA 416
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEK---IAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1750864354 417 CIYTDSGASVREFRENIESGMLGVNvGVPAPMAFFPFSGWKDSFYG 462
Cdd:PRK13968 396 TIFTTDETQARQMAARLECGGVFIN-GYCASDARVAFGGVKKSGFG 440
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
30-468 |
5.74e-62 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 208.82 E-value: 5.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 30 NPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQR 109
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 110 GIECVEFAAGAPTLMMGKQLPDI-ATGIESGMYRY-PIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLA 187
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADEPADAaAVGASRAYVRYqPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 188 ARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADL 267
Cdd:PRK09406 167 LYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 268 NVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGVEE 347
Cdd:PRK09406 247 DRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 348 GARLVRDGRedhAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVR 427
Cdd:PRK09406 327 GATILCGGK---RPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQE 403
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1750864354 428 EFRENIESGMLGVNvGVPAPMAFFPFSGWKDSFYG-DLHANG 468
Cdd:PRK09406 404 RFIDDLEAGQVFIN-GMTVSYPELPFGGVKRSGYGrELSAHG 444
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
13-413 |
3.89e-60 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 213.65 E-value: 3.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 13 IGGEwvdSSTSLTEPVYNPA-TGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:COG4230 562 IAGE---AASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMAL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEARGEVqRgiECVEF----AAGAPTLMmgkqlpdiatgiESGMYRYPIGVIGGITPfnfpmmvpcWMFPL 167
Cdd:COG4230 639 LVREAGKTLPDAIAEV-R--EAVDFcryyAAQARRLF------------AAPTVLRGRGVFVCISP---------WNFPL 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 168 AI---------ACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAey 237
Cdd:COG4230 695 AIftgqvaaalAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTETA-- 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 238 vykkgtenlKRVQ-ALAgAKNHSIV--------LN----D---------ADlnvatkqIIGAAFGSAGERCMAASVVTVQ 295
Cdd:COG4230 773 ---------RLINrTLA-ARDGPIVpliaetggQNamivDssalpeqvvDD-------VLASAFDSAGQRCSALRVLCVQ 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 296 EDVADELISRLV---QEsnnIVIGN--GLEKDVflGPVIRENHKERTLSYIEsgveegaRLVRDGREDHAVK-----ENG 365
Cdd:COG4230 836 EDIADRVLEMLKgamAE---LRVGDpaDLSTDV--GPVIDAEARANLEAHIE-------RMRAEGRLVHQLPlpeecANG 903
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1750864354 366 YFVGPTIF--DNVTQemkiWQDEIFAPVLSIVRVK--TLEEAIDVANNSRFA 413
Cdd:COG4230 904 TFVAPTLIeiDSISD----LEREVFGPVLHVVRYKadELDKVIDAINATGYG 951
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
9-412 |
4.71e-60 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 212.75 E-value: 4.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 9 VKNYIGGEW----VDSSTSLTEPVYNPA-TGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVD 83
Cdd:PRK11904 543 IAAFLEKQWqagpIINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 84 NWDELAKLVTLENGKSFNEARGEVQrgiECVEF----AAGAPTLM-MGKQLPDIaTGIESGMYRYPIGVIGGITPfnfpm 158
Cdd:PRK11904 623 NRAELIALCVREAGKTLQDAIAEVR---EAVDFcryyAAQARRLFgAPEKLPGP-TGESNELRLHGRGVFVCISP----- 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 159 mvpcWMFPLAI---------ACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISF 228
Cdd:PRK11904 694 ----WNFPLAIflgqvaaalAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAF 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 229 VGSqpvaeyvykkgTENLKRV-QALAgAKNHSIV--------LN----D--ADLNVATKQIIGAAFGSAGERCMAASVVT 293
Cdd:PRK11904 770 TGS-----------TETARIInRTLA-ARDGPIVpliaetggQNamivDstALPEQVVDDVVTSAFRSAGQRCSALRVLF 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 294 VQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIEsgveegaRLVRDGREDHAVK-----ENGYFV 368
Cdd:PRK11904 838 VQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIE-------RMKREARLLAQLPlpagtENGHFV 910
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1750864354 369 GPTIF--DNVTQemkiWQDEIFAPVLSIVRVKT--LEEAIDVANNSRF 412
Cdd:PRK11904 911 APTAFeiDSISQ----LEREVFGPILHVIRYKAsdLDKVIDAINATGY 954
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
19-455 |
6.87e-57 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 203.94 E-value: 6.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 19 DSSTSLTEPVYNPA-TGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENG 97
Cdd:PRK11905 562 GDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 98 KSFNEARGEVQrgiECVEF----AAGAPTLmmgkqlpdiatgiESGMYRYPIGVIGGITPfnfpmmvpcWMFPLAI---- 169
Cdd:PRK11905 642 KTLANAIAEVR---EAVDFlryyAAQARRL-------------LNGPGHKPLGPVVCISP---------WNFPLAIftgq 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 170 -----ACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKKGT 243
Cdd:PRK11905 697 iaaalVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQRTLA 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 244 ENLKRVQAL---AGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRL---VQEsnnIVIGN 317
Cdd:PRK11905 777 KRSGPPVPLiaeTGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLkgaMDE---LRIGD 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 318 GLEKDVFLGPVIRENHKERTLSYIESGVEEGARLVRDGREDHAvkENGYFVGPTIF--DNVTqEMKiwqDEIFAPVLSIV 395
Cdd:PRK11905 854 PWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAET--EKGTFVAPTLIeiDSIS-DLE---REVFGPVLHVV 927
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1750864354 396 RVKT--LEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVN-------VGVPapmaffPFSG 455
Cdd:PRK11905 928 RFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniigavVGVQ------PFGG 990
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
13-455 |
1.29e-55 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 193.20 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 13 IGGEWVDSSTSltEPVYNPAT-GEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:TIGR01238 42 IGHSYKADGEA--QPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDiatgiesgmyryPIGVIGGITPFNFPMMVPCWMFPLAIAC 171
Cdd:TIGR01238 120 CVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVE------------SRGVFVCISPWNFPLAIFTGQISAALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 172 GNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAEYVYK---KGTENLK 247
Cdd:TIGR01238 188 GNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRgADVGAALTSDPRIAGVAFTGSTEVAQLINQtlaQREDAPV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 248 RVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGP 327
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 328 VIRENHKERTLSYIESGVEEGARLVRDGREDHAVKENGYFVGPTIFDnvTQEMKIWQDEIFAPVLSIVRVKT--LEEAID 405
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVD 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1750864354 406 VANNSRFANGACIYTDSGASVREFRENIESGMLGVNVG-VPAPMAFFPFSG 455
Cdd:TIGR01238 426 QINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNqVGAVVGVQPFGG 476
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
12-485 |
1.67e-55 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 193.13 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEpvYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:PLN02315 24 YVGGEWRANGPLVSS--VNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEARGEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIAC 171
Cdd:PLN02315 102 VSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 172 GNTFVLKPSERTPLLA---ARLV-ELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLK 247
Cdd:PLN02315 182 GNCVVWKGAPTTPLITiamTKLVaEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 248 RVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGP 327
Cdd:PLN02315 262 KCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 328 VIRENHKERTLSYIESGVEEGARLVRDGRedhAVKENGYFVGPTIFDnVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVA 407
Cdd:PLN02315 342 LHTPESKKNFEKGIEIIKSQGGKILTGGS---AIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEIN 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 408 NNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMAFF--PFSGWKDSfyGDLHANGTDGVEFYTRKKMVTARY 485
Cdd:PLN02315 418 NSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIggAFGGEKAT--GGGREAGSDSWKQYMRRSTCTINY 495
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
43-481 |
3.89e-55 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 190.12 E-value: 3.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 43 STKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEAR-GEVQRGI-ECVEFAAGA 120
Cdd:cd07135 2 TPLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKnDILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 121 PTLMMGKQLPDIATGIESGMYRY---PIGVIGGITPFNFPMMVPcwMFPL--AIACGNTFVLKPSERTPLLAARLVELFE 195
Cdd:cd07135 82 KKWAKDEKVKDGPLAFMFGKPRIrkePLGVVLIIGPWNYPVLLA--LSPLvgAIAAGCTVVLKPSELTPHTAALLAELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 196 EAgLPKGVLNIVNGAHDVVNGLLEHKLVKaISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQII 275
Cdd:cd07135 160 KY-LDPDAFQVVQGGVPETTALLEQKFDK-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 276 GAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFlGPVIRENHKERTLSYIEsgvEEGARLVRDG 355
Cdd:cd07135 238 WGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLKSLLD---TTKGKVVIGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 356 REDHAVKengyFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIES 435
Cdd:cd07135 314 EMDEATR----FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRS 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1750864354 436 GMLGVN-----VGVPApmafFPFSGWKDSFYGDLHanGTDGVEFYTRKKMV 481
Cdd:cd07135 390 GGVVINdtlihVGVDN----APFGGVGDSGYGAYH--GKYGFDTFTHERTV 434
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
28-481 |
2.31e-53 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 186.09 E-value: 2.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 28 VYNPATGEVIAEVPLSTKADVDQAVQAANEAFK---GWskTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEAR 104
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 105 GEVQRGIECVEFAAGAPTLMMGKQLPDIATGIESG----MYRYPIGVIGGITPFNFPM------MVPcwmfplAIACGNT 174
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIPMGLTPASAGriafTTREPIGVVVAISAFNHPLnlivhqVAP------AIAAGCP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 175 FVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKK---GTenlkRVQA 251
Cdd:cd07148 155 VIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKlapGT----RCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 252 LAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRE 331
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 332 NHKERTLSYIESGVEEGARLVRDGREdhaVKENGYfvGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSR 411
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKR---LSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 412 FANGACIYTDsgasvrefreNIESGMLGVN------VGVPAPMAF----FPFSGWKDSFYgdlhanGTDGVEF----YTR 477
Cdd:cd07148 386 VAFQAAVFTK----------DLDVALKAVRrldataVMVNDHTAFrvdwMPFAGRRQSGY------GTGGIPYtmhdMTQ 449
|
....
gi 1750864354 478 KKMV 481
Cdd:cd07148 450 EKMA 453
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
13-410 |
1.70e-47 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 176.70 E-value: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 13 IGGEWVDSSTSltePVYNPA-TGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKL 91
Cdd:PRK11809 651 LEDPVAAGEMS---PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGL 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 92 VTLENGKSFNEARGEVQRGIECVEFAAGaptlmmgkqlpDIATGIESGMYRyPIGVIGGITPFNFPMMVPCWMFPLAIAC 171
Cdd:PRK11809 728 LVREAGKTFSNAIAEVREAVDFLRYYAG-----------QVRDDFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAA 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 172 GNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVV-NGLLEHKLVKAISFVGSQPVAEYVYKkgteNL-KRV 249
Cdd:PRK11809 796 GNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVARLLQR----NLaGRL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 250 Q---------ALAGAKNHSIVlndaDLNVATKQIIG----AAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIG 316
Cdd:PRK11809 872 DpqgrpipliAETGGQNAMIV----DSSALTEQVVAdvlaSAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMG 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 317 NG--LEKDVflGPVIRENHKERTLSYIESGVEEGARLVRDGREDHAVKENGYFVGPTI--FDNVtQEMKiwqDEIFAPVL 392
Cdd:PRK11809 948 NPdrLSTDI--GPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTLieLDSF-DELK---REVFGPVL 1021
|
410 420
....*....|....*....|
gi 1750864354 393 SIVRVK--TLEEAIDVANNS 410
Cdd:PRK11809 1022 HVVRYNrnQLDELIEQINAS 1041
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
70-481 |
5.12e-46 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 165.39 E-value: 5.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 70 RARILFKYQQLLVDNWDELAKLVTLENGKSFNEAR----GEVQRGIECVEfaagaptlmmgKQLPD----------IATG 135
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiAVVLGEIDHAL-----------KHLKKwmkprrvsvpLLLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 136 IESGMYRY-PIGVIGGITPFNFPMMVpCWMfPL--AIACGNTFVLKPSERTPLLAARLVELFEEAgLPKGVLNIVNGAHD 212
Cdd:cd07087 91 PAKAYVIPePLGVVLIIGPWNYPLQL-ALA-PLigAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 213 VVNGLLEHKLVKaISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVV 292
Cdd:cd07087 168 VATALLAEPFDH-IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 293 TVQEDVADELISRLVQESNNiVIGNGLEKDVFLGPVIRENHKERTLSYIESGveegaRLVRDGREDhavkENGYFVGPTI 372
Cdd:cd07087 247 LVHESIKDELIEELKKAIKE-FYGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGGQVD----KEERYIAPTI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 373 FDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVaNNSRFANGAC-IYTDSGASVREFRENIESGMLGVN-----VGVPA 446
Cdd:cd07087 317 LDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEF-INSRPKPLALyLFSEDKAVQERVLAETSSGGVCVNdvllhAAIPN 395
|
410 420 430
....*....|....*....|....*....|....*
gi 1750864354 447 pmafFPFSGWKDSFYGDLHanGTDGVEFYTRKKMV 481
Cdd:cd07087 396 ----LPFGGVGNSGMGAYH--GKAGFDTFSHLKSV 424
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
12-394 |
3.77e-44 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 162.37 E-value: 3.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 12 YIGGEWVDSSTSLTEPvyNPAT-GEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNW-DELA 89
Cdd:cd07123 36 VIGGKEVRTGNTGKQV--MPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 90 KLVTLENGKSFNEArgEVQRGIECVEF----AAGApTLMMGKQLPDIATGIESGM-YRYPIGVIGGITPFNFPmmvpcwm 164
Cdd:cd07123 114 AATMLGQGKNVWQA--EIDAACELIDFlrfnVKYA-EELYAQQPLSSPAGVWNRLeYRPLEGFVYAVSPFNFT------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 165 fplAIA---------CGNTFVLKPSErTPLLAARLV-ELFEEAGLPKGVLNIVNG-AHDVVNGLLEHKLVKAISFVGSQP 233
Cdd:cd07123 184 ---AIGgnlagapalMGNVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGdGPVVGDTVLASPHLAGLHFTGSTP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 234 VAEYVYKKGTENLK------RVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDVADELISRLV 307
Cdd:cd07123 260 TFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 308 QESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGVEE-GARLVRDGREDhavKENGYFVGPTIFDNVTQEMKIWQDE 386
Cdd:cd07123 340 EELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCD---DSVGYFVEPTVIETTDPKHKLMTEE 416
|
....*...
gi 1750864354 387 IFAPVLSI 394
Cdd:cd07123 417 IFGPVLTV 424
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
67-484 |
2.19e-42 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 157.11 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 67 VPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEA--------RGEVQRGIECV-EFAAGAPTLMMGKQLPDiatgiE 137
Cdd:PTZ00381 28 LEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkmtevlltVAEIEHLLKHLdEYLKPEKVDTVGVFGPG-----K 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 138 SGMYRYPIGVIGGITPFNFPM---MVPCwmfPLAIACGNTFVLKPSERTPLLAARLVELFEEAgLPKGVLNIVNGAHDVV 214
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLnltLIPL---AGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 215 NGLLEHKLvKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTV 294
Cdd:PTZ00381 179 TELLKEPF-DHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 295 QEDVADELISRLvQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIEsgvEEGARLVRDGREDHAVKengyFVGPTIFD 374
Cdd:PTZ00381 258 HRSIKDKFIEAL-KEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGGEVDIENK----YVAPTIIV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 375 NVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVAnNSRFANGAC-IYTDSGASVREFRENIESGMLGVN---VGVPAPMaf 450
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYENIDEVLEFI-NSRPKPLALyYFGEDKRHKELVLENTSSGAVVINdcvFHLLNPN-- 406
|
410 420 430
....*....|....*....|....*....|....
gi 1750864354 451 FPFSGWKDSFYGDLHanGTDGVEFYTRKKMVTAR 484
Cdd:PTZ00381 407 LPFGGVGNSGMGAYH--GKYGFDTFSHPKPVLNK 438
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
141-405 |
6.72e-41 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 152.27 E-value: 6.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 141 YRYPIGVIGGITPFNFPMMVPcwMFPL--AIACGNTFVLKPSERTPLLAARLVELFEEAgLPKGVLNIVNGAHDVVNGLL 218
Cdd:cd07136 97 YYEPYGVVLIIAPWNYPFQLA--LAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 219 EHKLVKaISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTVQEDV 298
Cdd:cd07136 174 DQKFDY-IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 299 ADELISRLVQESNNIVIGNGLEKDVFlGPVIRENHKERTLSYIESGveegaRLVRDGREDhavkENGYFVGPTIFDNVTQ 378
Cdd:cd07136 253 KEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLDNG-----KIVFGGNTD----RETLYIEPTILDNVTW 322
|
250 260
....*....|....*....|....*..
gi 1750864354 379 EMKIWQDEIFAPVLSIVRVKTLEEAID 405
Cdd:cd07136 323 DDPVMQEEIFGPILPVLTYDTLDEAIE 349
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
120-444 |
1.00e-39 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 148.53 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 120 APTLMMgkqlpdiaTGIESGMYRYPIGVIGGITPFNFPMMVPcwMFPL--AIACGNTFVLKPSERTPLLAARLVELFEEA 197
Cdd:cd07134 84 RTPLLL--------FGTKSKIRYEPKGVCLIISPWNYPFNLA--FGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 198 GLPKGVlNIVNGAHDVVNGLLE----HklvkaISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQ 273
Cdd:cd07134 154 FDEDEV-AVFEGDAEVAQALLElpfdH-----IFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 274 IIGAAFGSAGERCMAASVVTVQEDVADELISRLVQEsnnivIGNGLEKDVF------LGPVIRENHKERTLSYIESGVEE 347
Cdd:cd07134 228 IAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAE-----IEKFYGKDAArkaspdLARIVNDRHFDRLKGLLDDAVAK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 348 GARLVRDGREDhavkENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVR 427
Cdd:cd07134 303 GAKVEFGGQFD----AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVN 378
|
330
....*....|....*..
gi 1750864354 428 EFRENIESGMLGVNVGV 444
Cdd:cd07134 379 KVLARTSSGGVVVNDVV 395
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
144-481 |
8.35e-38 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 143.32 E-value: 8.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 144 PIGVIGGITPFNFPMMVPcwMFPL--AIACGNTFVLKPSERTPLLAARLVELFEEAgLPKGVLNIVNGAHDVVNGLLEHK 221
Cdd:cd07137 101 PLGVVLVISAWNFPFLLS--LEPVigAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETTALLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 222 LVKaISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGS-AGERCMAASVVTVQEDVAD 300
Cdd:cd07137 178 WDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESFAP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 301 ELISRLVQESNNIVIGNGLEKDVfLGPVIRENHKERtLSYIESGVEEGARLVRDGREDhavkENGYFVGPTIFDNVTQEM 380
Cdd:cd07137 257 TLIDALKNTLEKFFGENPKESKD-LSRIVNSHHFQR-LSRLLDDPSVADKIVHGGERD----EKNLYIEPTILLDPPLDS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 381 KIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVN-----VGVPApmafFPFSG 455
Cdd:cd07137 331 SIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtvvqYAIDT----LPFGG 406
|
330 340
....*....|....*....|....*.
gi 1750864354 456 WKDSFYGDLHanGTDGVEFYTRKKMV 481
Cdd:cd07137 407 VGESGFGAYH--GKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
48-435 |
2.91e-34 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 133.52 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 48 VDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGK----SFNEARGEVQ-RGIECVEFAAGAPT 122
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwmfAENICGDQVQlRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 123 LMMGKQLPDIATGIESgmYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAG-LPK 201
Cdd:cd07084 81 EPGNHLGQGLKQQSHG--YRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 202 GVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTEnlKRVQALAGAKNHSIVLNDAD-LNVATKQIIGAAFG 280
Cdd:cd07084 159 EDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 281 SAGERCMAASVVTVQED-----VADELISRLVQESnnivignglEKDVFLGPVIRENhkerTLSYIESGVEEGARLVR-D 354
Cdd:cd07084 237 CSGQKCTAQSMLFVPENwsktpLVEKLKALLARRK---------LEDLLLGPVQTFT----TLAMIAHMENLLGSVLLfS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 355 GREDHAVKEN---GYFVGPTIF---DNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANG--ACIYTDSGASV 426
Cdd:cd07084 304 GKELKNHSIPsiyGACVASALFvpiDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSltAAIYSNDPIFL 383
|
....*....
gi 1750864354 427 REFRENIES 435
Cdd:cd07084 384 QELIGNLWV 392
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
144-441 |
1.67e-33 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 131.45 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 144 PIGVIGGITPFNFPMMVPcwMFPL--AIACGNTFVLKPSERTPLLAARLVELFEEAGLPKgVLNIVNGAHDVVngllehk 221
Cdd:cd07133 101 PLGVVGIIVPWNYPLYLA--LGPLiaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADVA------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 222 lvKAIS--------FVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVT 293
Cdd:cd07133 171 --AAFSslpfdhllFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 294 VQEDVADELISRLVQESNNI---VIGNgleKDvfLGPVIRENHKERTLSYIESGVEEGARLVRDGREDHAVKENGYFVgP 370
Cdd:cd07133 249 VPEDKLEEFVAAAKAAVAKMyptLADN---PD--YTSIINERHYARLQGLLEDARAKGARVIELNPAGEDFAATRKLP-P 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1750864354 371 TIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAID-VanNSRFANGAC-IYTDSGASVREFRENIESGMLGVN 441
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDyI--NARPRPLALyYFGEDKAEQDRVLRRTHSGGVTIN 393
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
141-484 |
9.19e-30 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 120.79 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 141 YRYPIGVIGGITPFNFPMMVPcwMFPL--AIACGNTFVLKPSERTPLLAARLVELfeeagLPKGVLN----IVNGAHDVV 214
Cdd:cd07132 97 YKEPLGVVLIIGAWNYPLQLT--LVPLvgAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLDKecypVVLGGVEET 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 215 NGLLEHKLVKaISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFGSAGERCMAASVVTV 294
Cdd:cd07132 170 TELLKQRFDY-IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 295 QEDVADELISRLvQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESGveegaRLVRDGREDhavkENGYFVGPTIFD 374
Cdd:cd07132 249 TPEVQEKFVEAL-KKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGG-----KVAIGGQTD----EKERYIAPTVLT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 375 NVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVN-VGVPAPMAFFPF 453
Cdd:cd07132 319 DVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdTIMHYTLDSLPF 398
|
330 340 350
....*....|....*....|....*....|.
gi 1750864354 454 SGWKDSFYGDLHanGTDGVEFYTRKKMVTAR 484
Cdd:cd07132 399 GGVGNSGMGAYH--GKYSFDTFSHKRSCLVK 427
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
144-484 |
2.73e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 108.59 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 144 PIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAgLPKGVLNIVNGAHDVVNGLLEHKLV 223
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 224 KaISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDADLNVATKQIIGAAFG-SAGERCMAASVVTVQEDVADEL 302
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPKV 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 303 ISRLVQESNNIVIGNGLE-KDvfLGPVIRENHKERtLSYIESGVEEGARLVRDGREDhavKENgYFVGPTIFDNVTQEMK 381
Cdd:PLN02174 270 IDAMKKELETFYGKNPMEsKD--MSRIVNSTHFDR-LSKLLDEKEVSDKIVYGGEKD---REN-LKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 382 IWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVN-VGVPAPMAFFPFSGWKDSF 460
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGESG 422
|
330 340
....*....|....*....|....
gi 1750864354 461 YGDLHanGTDGVEFYTRKKMVTAR 484
Cdd:PLN02174 423 MGAYH--GKFSFDAFSHKKAVLYR 444
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
153-484 |
3.78e-25 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 107.89 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 153 PFNFPMMVPCWMFPL---------AIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVlNIVNGAHDVVNGLLEHKLV 223
Cdd:PLN02203 108 PLGVVLIFSSWNFPIglslepligAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV-KVIEGGPAVGEQLLQHKWD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 224 KaISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIV---LNDADLNVATKQIIGAAFGS-AGERCMAASVVTVQEDVA 299
Cdd:PLN02203 187 K-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 300 DELISRLVQESNNIVIGNGLEKDvFLGPVIRENHKERTLSYIESGVEEgARLVRDGREDhavkENGYFVGPTIFDNVTQE 379
Cdd:PLN02203 266 PILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSID----EKKLFIEPTILLNPPLD 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 380 MKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREFRENIESGMLGVNVGVPAPMA-FFPFSGWKD 458
Cdd:PLN02203 340 SDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACdSLPFGGVGE 419
|
330 340
....*....|....*....|....*.
gi 1750864354 459 SFYGDLHanGTDGVEFYTRKKMVTAR 484
Cdd:PLN02203 420 SGFGRYH--GKYSFDTFSHEKAVLRR 443
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
9-429 |
1.92e-23 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 103.12 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 9 VKNYIGGEWVDSSTSLTePVYNPATGEVIAEVPlSTKADVDQAVQAANEafkgwskTAVPK--------RARILFKYQQL 80
Cdd:cd07128 1 LQSYVAGQWHAGTGDGR-TLHDAVTGEVVARVS-SEGLDFAAAVAYARE-------KGGPAlraltfheRAAMLKALAKY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 81 LVDNWDELAKLVTLeNGKSFNEARGEVQRGIECVEFAAGaptlmMGKQLPDIATGIESG-----------MYRY---PI- 145
Cdd:cd07128 72 LMERKEDLYALSAA-TGATRRDSWIDIDGGIGTLFAYAS-----LGRRELPNAHFLVEGdveplskdgtfVGQHiltPRr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 146 GVIGGITPFNFPmmvpCW-M---FPLAIACGNTFVLKPSERTPLLAARLVELFEEAG-LPKGVLNIVNGAhdvVNGLLEH 220
Cdd:cd07128 146 GVAVHINAFNFP----VWgMlekFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS---VGDLLDH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 221 KLVK-AISFVGSQPVAeyvykkgtenlKRVQALAGAKNHSIVLN-DAD-LNVAtkqIIG--AAFGS-------------- 281
Cdd:cd07128 219 LGEQdVVAFTGSAATA-----------AKLRAHPNIVARSIRFNaEADsLNAA---ILGpdATPGTpefdlfvkevarem 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 282 ---AGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIESgVEEGARLVRDGRED 358
Cdd:cd07128 285 tvkAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDR 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1750864354 359 HAVK----ENGYFVGPTIF--DNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREF 429
Cdd:cd07128 364 FEVVgadaEKGAFFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAREL 440
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
10-429 |
9.19e-22 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 98.24 E-value: 9.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 10 KNYIGGEWVDSSTSLTePVYNPATGEVIAEVPlSTKADVDQAVQAANE----AFKGWSktaVPKRARILFKYQQLLVDNW 85
Cdd:PRK11903 6 ANYVAGRWQAGSGAGT-PLFDPVTGEELVRVS-ATGLDLAAAFAFAREqggaALRALT---YAQRAALLAAIVKVLQANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 86 DELAKLVTLENGKSFNEARGEVQRGIECVEFAAgaptlMMGKQLPDIATGIESGMYRY-------------PI-GVIGGI 151
Cdd:PRK11903 81 DAYYDIATANSGTTRNDSAVDIDGGIFTLGYYA-----KLGAALGDARLLRDGEAVQLgkdpafqgqhvlvPTrGVALFI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 152 TPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAG-LPKGVLNIVNGAHdvvNGLLEH-KLVKAISFV 229
Cdd:PRK11903 156 NAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSS---AGLLDHlQPFDVVSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 230 GSQPVAEYVYKKG--TENLKRVQALAGAKNHSIVLNDAD-----LNVATKQIIGAAFGSAGERCMAASVVTVQEDVADEL 302
Cdd:PRK11903 233 GSAETAAVLRSHPavVQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 303 ISRLVQESNNIVIGNGLEKDVFLGPVIRENHKERTLSYIEsGVEEGARLVRDGREDHAVKEN---GYFVGPTIF-----D 374
Cdd:PRK11903 313 AEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDADpavAACVGPTLLgasdpD 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1750864354 375 NVTqemKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANGACIYTDSGASVREF 429
Cdd:PRK11903 392 AAT---AVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAA 443
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
11-390 |
2.22e-19 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 90.63 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 11 NYIGGEWVDSSTSLTepVYNPATGEVIAEVPLSTKADVDQAVQAANEAFKGWSKTAV--PKR--------ARILFKYQQL 80
Cdd:cd07126 1 NLVAGKWKGASNYTT--LLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLknPERyllygdvsHRVAHELRKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 81 LVDnwDELAKLVTLENGKSFNEARGEV---QRGIEcvEFAAGAPTLMM-GKQLPDIATGIESGMYRYPIGVIGGITPFNF 156
Cdd:cd07126 79 EVE--DFFARLIQRVAPKSDAQALGEVvvtRKFLE--NFAGDQVRFLArSFNVPGDHQGQQSSGYRWPYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 157 PMMVPCWMFPLAIACGNTFVLKPSERTPLLAARLVELFEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAE 236
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 237 YvykkgtenlkrvqaLAGAKNHSIVLNDA------------DLNVATKQIIGAAFGSAGERCMAASVVTVQEDVAD---- 300
Cdd:cd07126 235 R--------------LALELHGKVKLEDAgfdwkilgpdvsDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQagil 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 301 ELISRLVQESNnivigngLEkDVFLGPVIRENhKERTLSYIESGVE-EGARLVRDGRE--DH-------AVKENGYFVgP 370
Cdd:cd07126 301 DKLKALAEQRK-------LE-DLTIGPVLTWT-TERILDHVDKLLAiPGAKVLFGGKPltNHsipsiygAYEPTAVFV-P 370
|
410 420
....*....|....*....|
gi 1750864354 371 TIFDNVTQEMKIWQDEIFAP 390
Cdd:cd07126 371 LEEIAIEENFELVTTEVFGP 390
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
46-407 |
6.90e-19 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 88.83 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 46 ADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGksfneaRGEVQRGIECVEFAAgaptlmm 125
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG------MGRVEDKIAKNHLAA------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 126 gKQLP---DIATGIESG-----MYRY-PIGVIGGITPF---------NFPMMvpcwmfplaIACGNTFVLKPSERTPLLA 187
Cdd:cd07121 71 -EKTPgteDLTTTAWSGdngltLVEYaPFGVIGAITPStnptetiinNSISM---------LAAGNAVVFNPHPGAKKVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 188 ARLVELFEEA-----GLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGtenlKRVQAlAGAKNHSIVL 262
Cdd:cd07121 141 AYAVELINKAiaeagGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSG----KKAIG-AGAGNPPVVV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 263 ND-ADLNVATKQII-GAAFGSaGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEK---DVFLGPvirenhkert 337
Cdd:cd07121 216 DEtADIEKAARDIVqGASFDN-NLPCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQlleVVLLTN---------- 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1750864354 338 lsyiesgveEGARLVRD--GREDHAV-KENGYFVGPT---IFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDVA 407
Cdd:cd07121 285 ---------KGATPNKKwvGKDASKIlKAAGIEVPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
46-407 |
9.41e-19 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 88.42 E-value: 9.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 46 ADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENG---------KsfNEARGEVQRGIECVEf 116
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedkiaK--NVAAAEKTPGVEDLT- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 117 aagaptlmmgkqlPDIATGiESGM--YRY-PIGVIGGITPFNFP---------MMvpcwmfplaIACGNTFVLKPSERTP 184
Cdd:PRK15398 113 -------------TEALTG-DNGLtlIEYaPFGVIGAVTPSTNPtetiinnaiSM---------LAAGNSVVFSPHPGAK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 185 LLAARLVELFEEA----GLPKGVLNIVNGAH-DVVNGLLEHKLVKAISFVGSQPVAEYVYKKGtenlKRVQAlAGAKNHS 259
Cdd:PRK15398 170 KVSLRAIELLNEAivaaGGPENLVVTVAEPTiETAQRLMKHPGIALLVVTGGPAVVKAAMKSG----KKAIG-AGAGNPP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 260 IVLND-ADLNVATKQII-GAAFGSaGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEK--DVFLGPVIRENHK- 334
Cdd:PRK15398 245 VVVDEtADIEKAARDIVkGASFDN-NLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKlqKVVLKNGGTVNKKw 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 335 -ERTLSYI--ESGVE--EGARLVrdgredhavkengyfVGPTIFDN--VTQEMKIwqdeifaPVLSIVRVKTLEEAIDVA 407
Cdd:PRK15398 324 vGKDAAKIleAAGINvpKDTRLL---------------IVETDANHpfVVTELMM-------PVLPVVRVKDVDEAIALA 381
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
48-408 |
3.23e-15 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 77.58 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 48 VDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGksFNEARGEVQRGIECVEFAAGAPTLMMG- 126
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQGELGRTTGQLRLFADLVREGs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 127 -------KQLPDIATGIESGMYRY--PIGVIGGITPFNFPMM--VPCWMFPLAIACGNTFVLK--PSE-RTPLLAARLV- 191
Cdd:cd07129 79 wldaridPADPDRQPLPRPDLRRMlvPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAHpGTSELVARAIr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 192 ELFEEAGLPKGVLNIVNGA-HDVVNGLLEHKLVKAISFVGSQPVAeyvykkgtenlKRVQALAGAKNHSI---------- 260
Cdd:cd07129 159 AALRATGLPAGVFSLLQGGgREVGVALVKHPAIKAVGFTGSRRGG-----------RALFDAAAARPEPIpfyaelgsvn 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 261 --VLNDADLNVATKQIIGAAFGS----AGERCMAASVVTVQEDVA-DELISRLVQESNNIVIGnglekdVFLGPVIREnh 333
Cdd:cd07129 228 pvFILPGALAERGEAIAQGFVGSltlgAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQ------TMLTPGIAE-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 334 kertlSYiESGVEE-----GARLVRDGredhAVKENGYFVGPTIFD-NVTQEMK--IWQDEIFAPVLSIVRVKTLEEAID 405
Cdd:cd07129 300 -----AY-RQGVEAlaaapGVRVLAGG----AAAEGGNQAAPTLFKvDAAAFLAdpALQEEVFGPASLVVRYDDAAELLA 369
|
...
gi 1750864354 406 VAN 408
Cdd:cd07129 370 VAE 372
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
48-421 |
4.91e-13 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 70.76 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 48 VDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSF-------NEARGEVQRGIECVEFAAGa 120
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRvedkvikNHFAAEYIYNVYKDEKTCG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 121 ptlMMGKQLPDIATGIESgmyryPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSER----TPLLAARLVELFEE 196
Cdd:cd07081 80 ---VLTGDENGGTLIIAE-----PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRakkvTQRAATLLLQAAVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 197 AGLPKGVLN-IVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGtenlKRVQAlAGAKNHSIVLND-ADLNVATKQI 274
Cdd:cd07081 152 AGAPENLIGwIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSG----KPAIG-VGAGNTPVVIDEtADIKRAVQSI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 275 IGAAFGSAGERCMAASVVTVQEDVADELISRLVQESNNIVIGNGLEKdvfLGPVIRENhkertlsyiesgVEEGARLVrd 354
Cdd:cd07081 227 VKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQ---VQPVILKN------------GDVNRDIV-- 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1750864354 355 GREDHAVKENGYFVGPT----IFDNVTQ--EMKIWQDEIFAPVLSIVRVKTLEEAIDVANNSRFANG----ACIYTD 421
Cdd:cd07081 290 GQDAYKIAAAAGLKVPQetriLIGEVTSlaEHEPFAHEKLSPVLAMYRAANFADADAKALALKLEGGcghtSAMYSD 366
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
53-306 |
9.92e-10 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 60.31 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 53 QAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEARGEVQRGIECVEFA-----------AGAP 121
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKlyknidtergiTASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 122 TLMMGKQLPDiatGIESGMYRYPIGVIGGITPFNFPMMVPCWMFpLAIACGNTFVLKPSERTPLLAARLVELFEEA---G 198
Cdd:cd07077 81 GHIQDVLLPD---NGETYVRAFPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 199 LPKGVLNIVNGAHD-VVNGLLEHKLVKAISFVGSQPVAEYVYKKGteNLKRVQALAGAKNHSIVLNDADLNVATKQIIGA 277
Cdd:cd07077 157 GPKILVLYVPHPSDeLAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260
....*....|....*....|....*....
gi 1750864354 278 AFgSAGERCMAASVVTVQEDVADELISRL 306
Cdd:cd07077 235 KF-FDQNACASEQNLYVVDDVLDPLYEEF 262
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
45-431 |
2.41e-09 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 59.41 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 45 KADVDQAVQAANEAFKGWSKTAVPKRARILFKYQQLLVDNWDELAKLVTLENGKSFNEA-----RGEVQRGIECVEFAAg 119
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfqaggPHAQDRGLEAVAYAW- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 120 aptlMMGKQLPDIATGIESGMYRYPIGVIGGIT--PFNFPMMVPCWMFPL---------AIACGNTFVLKPSERTPLLAA 188
Cdd:cd07127 162 ----REMSRIPPTAEWEKPQGKHDPLAMEKTFTvvPRGVALVIGCSTFPTwngypglfaSLATGNPVIVKPHPAAILPLA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 189 RLV----ELFEEAGLPKGVLNIV--NGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTEnlKRVQALAGAKNHSIVL 262
Cdd:cd07127 238 ITVqvarEVLAEAGFDPNLVTLAadTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 263 NDADLNVATKQIigaAFGSA---GERCMAASVVTVQED---------VADELISRLVQESNNIvIGNGLEKDVFLGPVIR 330
Cdd:cd07127 316 STDDLKAMLRNL---AFSLSlysGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADPARAAALLGAIQS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 331 ENHKERtlsyiesgVEEGARL---VRDGRE-DHAVKENGYFVGPTIFDNVTQEMKIWQDEIFAPVLSIVRVKTLEEAIDV 406
Cdd:cd07127 392 PDTLAR--------IAEARQLgevLLASEAvAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIEL 463
|
410 420
....*....|....*....|....*...
gi 1750864354 407 ANNSRFANGAC---IYTDSGASVREFRE 431
Cdd:cd07127 464 ARESVREHGAMtvgVYSTDPEVVERVQE 491
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
144-441 |
1.95e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 50.18 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 144 PIGVIGGITPFNFPMMVPcwMFP--LAIACGNTFVLKPSER---TPLLAARLV-ELFEEAGLPKGVLNIVNGA-HDVVNG 216
Cdd:cd07122 95 PVGVIAALIPSTNPTSTA--IFKalIALKTRNAIIFSPHPRakkCSIEAAKIMrEAAVAAGAPEGLIQWIEEPsIELTQE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 217 LLEHKLVKAISFVGSQPVAEYVYKKGTEnlkrvqALA-GAKNHSIVLN-DADLNVATKQII-GAAF--GSAgerCMAASV 291
Cdd:cd07122 173 LMKHPDVDLILATGGPGMVKAAYSSGKP------AIGvGPGNVPAYIDeTADIKRAVKDIIlSKTFdnGTI---CASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 292 VTVQEDVADELISRLvqESNNIVIGNGLEKDVFLGPVIRENHK------ERTLSYI--ESGVE--EGARLVrdgredhAV 361
Cdd:cd07122 244 VIVDDEIYDEVRAEL--KRRGAYFLNEEEKEKLEKALFDDGGTlnpdivGKSAQKIaeLAGIEvpEDTKVL-------VA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750864354 362 KENGyfVGPTIfdnvtqemkIWQDEIFAPVLSIVRVKTLEEAIDVA----NNSRFANGACIYTDSGASVREFRENIESGM 437
Cdd:cd07122 315 EETG--VGPEE---------PLSREKLSPVLAFYRAEDFEEALEKArellEYGGAGHTAVIHSNDEEVIEEFALRMPVSR 383
|
....
gi 1750864354 438 LGVN 441
Cdd:cd07122 384 ILVN 387
|
|
| |
